Study of structure-function relationships in the plant cell wall and modifications of the wall structure by enzyme engineering

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info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173017/RS//

Study of structure-function relationships in the plant cell wall and modifications of the wall structure by enzyme engineering (en)
Испитивања односа структура-функција у ћелијском зиду биљака и измене структуре зида ензимским инжењерингом (sr)
Ispitivanja odnosa struktura-funkcija u ćelijskom zidu biljaka i izmene strukture zida enzimskim inženjeringom (sr_RS)
Authors

Publications

Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls

Ilić Đurđić, Karla; Ostafe, Raluca; Prodanović, Olivera; Đurđević Đelmaš, Aleksandra; Popović, Nikolina; Fischer, Rainer; Schillberg, Stefan; Prodanović, Radivoje

(Springer, 2021)

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4101
AB  - The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) from Phanerochaete chrysosporium is a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 104 independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.
PB  - Springer
T2  - Frontiers of Environmental Science & Engineering
T2  - Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
T1  - Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls
VL  - 15
IS  - 2
SP  - 19
DO  - 10.1007/s11783-020-1311-4
ER  - 
@article{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Prodanović, Olivera and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
abstract = "The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) from Phanerochaete chrysosporium is a heme-containing lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules, including industrial dyes. This enzyme is therefore ideal as a starting point for protein engineering. Accordingly, we subjected two positions (165 and 264) in the environment of the catalytic Trp171 residue to saturation mutagenesis, and the resulting library of 104 independent clones was expressed on the surface of yeast cells. This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently. We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes (Evans blue, amido black 10B and Guinea green) and up to 13-fold higher catalytic activity. Additionally, cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis, achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst. LiP-coated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h. The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.",
publisher = "Springer",
journal = "Frontiers of Environmental Science & Engineering, Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.",
title = "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls",
volume = "15",
number = "2",
pages = "19",
doi = "10.1007/s11783-020-1311-4"
}
Ilić Đurđić, K., Ostafe, R., Prodanović, O., Đurđević Đelmaš, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R.. (2021). Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering
Springer., 15(2), 19.
https://doi.org/10.1007/s11783-020-1311-4
Ilić Đurđić K, Ostafe R, Prodanović O, Đurđević Đelmaš A, Popović N, Fischer R, Schillberg S, Prodanović R. Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering. 2021;15(2):19.
doi:10.1007/s11783-020-1311-4 .
Ilić Đurđić, Karla, Ostafe, Raluca, Prodanović, Olivera, Đurđević Đelmaš, Aleksandra, Popović, Nikolina, Fischer, Rainer, Schillberg, Stefan, Prodanović, Radivoje, "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls" in Frontiers of Environmental Science & Engineering, 15, no. 2 (2021):19,
https://doi.org/10.1007/s11783-020-1311-4 . .
4
4
4

Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4

Ilić Đurđić, Karla; Ostafe, Raluca; Prodanović, Olivera; Đurđević Đelmaš, Aleksandra; Popović, Nikolina; Fischer, Rainer; Schillberg, Stefan; Prodanović, Radivoje

(Springer, 2021)

TY  - DATA
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4103
PB  - Springer
T2  - Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
T1  - Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4
ER  - 
@misc{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Prodanović, Olivera and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
publisher = "Springer",
journal = "Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.",
title = "Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4"
}
Ilić Đurđić, K., Ostafe, R., Prodanović, O., Đurđević Đelmaš, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R.. (2021). Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4. in Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.
Springer..
Ilić Đurđić K, Ostafe R, Prodanović O, Đurđević Đelmaš A, Popović N, Fischer R, Schillberg S, Prodanović R. Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4. in Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.. 2021;..
Ilić Đurđić, Karla, Ostafe, Raluca, Prodanović, Olivera, Đurđević Đelmaš, Aleksandra, Popović, Nikolina, Fischer, Rainer, Schillberg, Stefan, Prodanović, Radivoje, "Supplementary data for the article: Ilić Đurđić, K.; Ostafe, R.; Prodanović, O.; Đurđević Đelmaš, A.; Popović, N.; Fischer, R.; Schillberg, S.; Prodanović, R. Improved Degradation of Azo Dyes by Lignin Peroxidase Following Mutagenesis at Two Sites near the Catalytic Pocket and the Application of Peroxidase-Coated Yeast Cell Walls. Front. Environ. Sci. Eng. 2020, 15 (2), 19. https://doi.org/10.1007/s11783-020-1311-4" in Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng. (2021).

Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls

Ilić Đurđić, Karla; Ostafe, Raluca; Đurđević Đelmaš, Aleksandra; Popović, Nikolina; Schillberg, Stefan; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2020)

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3835
AB  - Azo dyes are toxic and carcinogenic synthetic pigments that accumulate as pollutants in aquatic bodies near textile factories. The pigments are structurally diverse, and bioremediation is mostly limited to single dye compounds or related groups. Versatile peroxidase (VP) from Pleurotus eryngii is a heme-containing peroxidase with a broad substrate spectrum that can break down many structurally distinct pollutants, including azo dyes. The utilization of this enzyme could be facilitated by engineering to modify its catalytic activity and substrate range. We used saturation mutagenesis to alter two amino acids in the catalytic tryptophan environment of VP (V160 and A260). Library screening with three azo dyes revealed that these two positions had a significant influence on substrate specificity. We were able to isolate and sequence VP variants with up to 16-fold higher catalytic efficiency for different azo dyes. The same approach could be used to select for VP variants that catalyze the degradation of many other types of pollutants. To allow multiple cycles of dye degradation, we immobilized VP on the surface of yeast cells and used washed cell wall fragments after lysis. VP embedded in the cell wall retained ∼70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h, making this platform ideal for the bioremediation of environments contaminated with azo dyes.
PB  - Elsevier
T2  - Enzyme and Microbial Technology
T1  - Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls
VL  - 136
SP  - e109509
DO  - 10.1016/j.enzmictec.2020.109509
ER  - 
@article{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Azo dyes are toxic and carcinogenic synthetic pigments that accumulate as pollutants in aquatic bodies near textile factories. The pigments are structurally diverse, and bioremediation is mostly limited to single dye compounds or related groups. Versatile peroxidase (VP) from Pleurotus eryngii is a heme-containing peroxidase with a broad substrate spectrum that can break down many structurally distinct pollutants, including azo dyes. The utilization of this enzyme could be facilitated by engineering to modify its catalytic activity and substrate range. We used saturation mutagenesis to alter two amino acids in the catalytic tryptophan environment of VP (V160 and A260). Library screening with three azo dyes revealed that these two positions had a significant influence on substrate specificity. We were able to isolate and sequence VP variants with up to 16-fold higher catalytic efficiency for different azo dyes. The same approach could be used to select for VP variants that catalyze the degradation of many other types of pollutants. To allow multiple cycles of dye degradation, we immobilized VP on the surface of yeast cells and used washed cell wall fragments after lysis. VP embedded in the cell wall retained ∼70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h, making this platform ideal for the bioremediation of environments contaminated with azo dyes.",
publisher = "Elsevier",
journal = "Enzyme and Microbial Technology",
title = "Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls",
volume = "136",
pages = "e109509",
doi = "10.1016/j.enzmictec.2020.109509"
}
Ilić Đurđić, K., Ostafe, R., Đurđević Đelmaš, A., Popović, N., Schillberg, S., Fischer, R.,& Prodanović, R.. (2020). Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls. in Enzyme and Microbial Technology
Elsevier., 136, e109509.
https://doi.org/10.1016/j.enzmictec.2020.109509
Ilić Đurđić K, Ostafe R, Đurđević Đelmaš A, Popović N, Schillberg S, Fischer R, Prodanović R. Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls. in Enzyme and Microbial Technology. 2020;136:e109509.
doi:10.1016/j.enzmictec.2020.109509 .
Ilić Đurđić, Karla, Ostafe, Raluca, Đurđević Đelmaš, Aleksandra, Popović, Nikolina, Schillberg, Stefan, Fischer, Rainer, Prodanović, Radivoje, "Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls" in Enzyme and Microbial Technology, 136 (2020):e109509,
https://doi.org/10.1016/j.enzmictec.2020.109509 . .
12
6
7

Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls

Ilić Đurđić, Karla; Ostafe, Raluca; Đurđević Đelmaš, Aleksandra; Popović, Nikolina; Schillberg, Stefan; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2020)

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3834
AB  - Azo dyes are toxic and carcinogenic synthetic pigments that accumulate as pollutants in aquatic bodies near textile factories. The pigments are structurally diverse, and bioremediation is mostly limited to single dye compounds or related groups. Versatile peroxidase (VP) from Pleurotus eryngii is a heme-containing peroxidase with a broad substrate spectrum that can break down many structurally distinct pollutants, including azo dyes. The utilization of this enzyme could be facilitated by engineering to modify its catalytic activity and substrate range. We used saturation mutagenesis to alter two amino acids in the catalytic tryptophan environment of VP (V160 and A260). Library screening with three azo dyes revealed that these two positions had a significant influence on substrate specificity. We were able to isolate and sequence VP variants with up to 16-fold higher catalytic efficiency for different azo dyes. The same approach could be used to select for VP variants that catalyze the degradation of many other types of pollutants. To allow multiple cycles of dye degradation, we immobilized VP on the surface of yeast cells and used washed cell wall fragments after lysis. VP embedded in the cell wall retained ∼70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h, making this platform ideal for the bioremediation of environments contaminated with azo dyes.
PB  - Elsevier
T2  - Enzyme and Microbial Technology
T1  - Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls
VL  - 136
SP  - e109509
DO  - 10.1016/j.enzmictec.2020.109509
ER  - 
@article{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Azo dyes are toxic and carcinogenic synthetic pigments that accumulate as pollutants in aquatic bodies near textile factories. The pigments are structurally diverse, and bioremediation is mostly limited to single dye compounds or related groups. Versatile peroxidase (VP) from Pleurotus eryngii is a heme-containing peroxidase with a broad substrate spectrum that can break down many structurally distinct pollutants, including azo dyes. The utilization of this enzyme could be facilitated by engineering to modify its catalytic activity and substrate range. We used saturation mutagenesis to alter two amino acids in the catalytic tryptophan environment of VP (V160 and A260). Library screening with three azo dyes revealed that these two positions had a significant influence on substrate specificity. We were able to isolate and sequence VP variants with up to 16-fold higher catalytic efficiency for different azo dyes. The same approach could be used to select for VP variants that catalyze the degradation of many other types of pollutants. To allow multiple cycles of dye degradation, we immobilized VP on the surface of yeast cells and used washed cell wall fragments after lysis. VP embedded in the cell wall retained ∼70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h, making this platform ideal for the bioremediation of environments contaminated with azo dyes.",
publisher = "Elsevier",
journal = "Enzyme and Microbial Technology",
title = "Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls",
volume = "136",
pages = "e109509",
doi = "10.1016/j.enzmictec.2020.109509"
}
Ilić Đurđić, K., Ostafe, R., Đurđević Đelmaš, A., Popović, N., Schillberg, S., Fischer, R.,& Prodanović, R.. (2020). Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls. in Enzyme and Microbial Technology
Elsevier., 136, e109509.
https://doi.org/10.1016/j.enzmictec.2020.109509
Ilić Đurđić K, Ostafe R, Đurđević Đelmaš A, Popović N, Schillberg S, Fischer R, Prodanović R. Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls. in Enzyme and Microbial Technology. 2020;136:e109509.
doi:10.1016/j.enzmictec.2020.109509 .
Ilić Đurđić, Karla, Ostafe, Raluca, Đurđević Đelmaš, Aleksandra, Popović, Nikolina, Schillberg, Stefan, Fischer, Rainer, Prodanović, Radivoje, "Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls" in Enzyme and Microbial Technology, 136 (2020):e109509,
https://doi.org/10.1016/j.enzmictec.2020.109509 . .
12
6
7

Ferrous iron binding to epinephrine promotes the oxidation of iron and impedes activation of adrenergic receptors

Korać Jačić, Jelena; Nikolić, Ljiljana; Stanković, Dalibor; Opačić, Miloš; Dimitrijević, Milena; Savić, Danijela; Grgurić-Šipka, Sanja; Spasojević, Ivan; Bogdanović Pristov, Jelena

(Elsevier, 2020)

TY  - JOUR
AU  - Korać Jačić, Jelena
AU  - Nikolić, Ljiljana
AU  - Stanković, Dalibor
AU  - Opačić, Miloš
AU  - Dimitrijević, Milena
AU  - Savić, Danijela
AU  - Grgurić-Šipka, Sanja
AU  - Spasojević, Ivan
AU  - Bogdanović Pristov, Jelena
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3809
AB  - Upon release in response to stress, epinephrine (Epi) may interact with labile iron pool in human plasma with potentially important (patho)physiological consequences. We have shown that Epi and Fe3+ build stable 1:1 high-spin bidentate complex at physiological pH, and that Epi does not undergo degradation in the presence of iron. However, the interactions of Epi with the more soluble Fe2+, and the impact of iron on biological activity of Epi are still not known. Herein we showed that Epi and Fe2+ build colorless complex which is stable under anaerobic conditions. In the presence of O2, Epi promoted the oxidation of Fe2+ and the formation of Epi-Fe3+ complex. Cyclic voltammetry showed that mid-point potential of Epi-Fe2+ complex is very low (−582 mV vs. standard hydrogen electrode), which explains catalyzed oxidation of Fe2+. Next, we examined the impact of iron binding on biological performance of Epi using patch clamping in cell culture with constitutive expression of adrenergic receptors. Epi alone evoked an increase of outward currents, whereas Epi in the complex with Fe3+ did not. This implies that the binding of Epi to adrenergic receptors and their activation is prevented by the formation of complex with iron. Pro-oxidative activity of Epi-Fe2+ complex may represent a link between chronic stress and cardiovascular problems. On the other hand, labile iron could serve as a modulator of biological activity of ligands. Such interactions may be important in human pathologies that are related to iron overload or deficiency.
PB  - Elsevier
T2  - Free Radical Biology and Medicine
T1  - Ferrous iron binding to epinephrine promotes the oxidation of iron and impedes activation of adrenergic receptors
VL  - 148
SP  - 123
EP  - 127
DO  - 10.1016/j.freeradbiomed.2020.01.001
ER  - 
@article{
author = "Korać Jačić, Jelena and Nikolić, Ljiljana and Stanković, Dalibor and Opačić, Miloš and Dimitrijević, Milena and Savić, Danijela and Grgurić-Šipka, Sanja and Spasojević, Ivan and Bogdanović Pristov, Jelena",
year = "2020",
abstract = "Upon release in response to stress, epinephrine (Epi) may interact with labile iron pool in human plasma with potentially important (patho)physiological consequences. We have shown that Epi and Fe3+ build stable 1:1 high-spin bidentate complex at physiological pH, and that Epi does not undergo degradation in the presence of iron. However, the interactions of Epi with the more soluble Fe2+, and the impact of iron on biological activity of Epi are still not known. Herein we showed that Epi and Fe2+ build colorless complex which is stable under anaerobic conditions. In the presence of O2, Epi promoted the oxidation of Fe2+ and the formation of Epi-Fe3+ complex. Cyclic voltammetry showed that mid-point potential of Epi-Fe2+ complex is very low (−582 mV vs. standard hydrogen electrode), which explains catalyzed oxidation of Fe2+. Next, we examined the impact of iron binding on biological performance of Epi using patch clamping in cell culture with constitutive expression of adrenergic receptors. Epi alone evoked an increase of outward currents, whereas Epi in the complex with Fe3+ did not. This implies that the binding of Epi to adrenergic receptors and their activation is prevented by the formation of complex with iron. Pro-oxidative activity of Epi-Fe2+ complex may represent a link between chronic stress and cardiovascular problems. On the other hand, labile iron could serve as a modulator of biological activity of ligands. Such interactions may be important in human pathologies that are related to iron overload or deficiency.",
publisher = "Elsevier",
journal = "Free Radical Biology and Medicine",
title = "Ferrous iron binding to epinephrine promotes the oxidation of iron and impedes activation of adrenergic receptors",
volume = "148",
pages = "123-127",
doi = "10.1016/j.freeradbiomed.2020.01.001"
}
Korać Jačić, J., Nikolić, L., Stanković, D., Opačić, M., Dimitrijević, M., Savić, D., Grgurić-Šipka, S., Spasojević, I.,& Bogdanović Pristov, J.. (2020). Ferrous iron binding to epinephrine promotes the oxidation of iron and impedes activation of adrenergic receptors. in Free Radical Biology and Medicine
Elsevier., 148, 123-127.
https://doi.org/10.1016/j.freeradbiomed.2020.01.001
Korać Jačić J, Nikolić L, Stanković D, Opačić M, Dimitrijević M, Savić D, Grgurić-Šipka S, Spasojević I, Bogdanović Pristov J. Ferrous iron binding to epinephrine promotes the oxidation of iron and impedes activation of adrenergic receptors. in Free Radical Biology and Medicine. 2020;148:123-127.
doi:10.1016/j.freeradbiomed.2020.01.001 .
Korać Jačić, Jelena, Nikolić, Ljiljana, Stanković, Dalibor, Opačić, Miloš, Dimitrijević, Milena, Savić, Danijela, Grgurić-Šipka, Sanja, Spasojević, Ivan, Bogdanović Pristov, Jelena, "Ferrous iron binding to epinephrine promotes the oxidation of iron and impedes activation of adrenergic receptors" in Free Radical Biology and Medicine, 148 (2020):123-127,
https://doi.org/10.1016/j.freeradbiomed.2020.01.001 . .

Variations in polyamine conjugates in maize (Zea mays L.) seeds contaminated with aflatoxin B1: a dose–response relationship

Bartolić, Dragana; Maksimović, Vuk; Maksimović, Jelena D.; Stanković, Mira; Krstović, Saša; Baošić, Rada; Radotić, Ksenija

(Wiley, 2020)

TY  - JOUR
AU  - Bartolić, Dragana
AU  - Maksimović, Vuk
AU  - Maksimović, Jelena D.
AU  - Stanković, Mira
AU  - Krstović, Saša
AU  - Baošić, Rada
AU  - Radotić, Ksenija
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3949
AB  - BACKGROUND: Cereal seeds, such as maize seeds, are frequently contaminated with aflatoxin B1 (AFB1), one of the most dangerous naturally occurring carcinogens. In plants, phenolamides are involved in biotic stress response. The data on variations of phenolamides in AFB1-containing seeds are limited. RESULTS: Five polyamine conjugates, including two spermidine and three putrescine conjugates, were tentatively identified in methanolic extracts, using HPLC-DAD-MS. The ratio of putrescine to spermidine conjugates changed with increasing AFB1 concentration in a logistic dose–response manner, with a ratio of below 1 up to a concentration of 51.51 μg kg−1, and approximately 2.54 and 3 at higher concentrations of 177.4 and 308.13 μg kg−1, respectively. The observed variations of the total antioxidant activity and the total phenolic content may support this biphasic behaviour of the seeds against AFB1 stress. CONCLUSIONS: The obtained data are a contribution to the understanding of the roles of polyamine conjugates in seed defence to increasing AFB1 concentrations. According to our knowledge, this study reports for the first time the biphasic response of maize seeds to increasing AFB1 contamination level, comprising the induction of polyamine conjugate accumulation and variation in the ratio of conjugates. This dose–response relationship may provide useful information in the field of agricultural and food chemistry as an indicator of AFB1 contamination level and, hence, for selecting an appropriate seed quality.
PB  - Wiley
T2  - Journal of the Science of Food and Agriculture
T1  - Variations in polyamine conjugates in maize (Zea mays L.) seeds contaminated with aflatoxin B1: a dose–response relationship
VL  - 100
IS  - 7
SP  - 2905
EP  - 2910
DO  - 10.1002/jsfa.10317
ER  - 
@article{
author = "Bartolić, Dragana and Maksimović, Vuk and Maksimović, Jelena D. and Stanković, Mira and Krstović, Saša and Baošić, Rada and Radotić, Ksenija",
year = "2020",
abstract = "BACKGROUND: Cereal seeds, such as maize seeds, are frequently contaminated with aflatoxin B1 (AFB1), one of the most dangerous naturally occurring carcinogens. In plants, phenolamides are involved in biotic stress response. The data on variations of phenolamides in AFB1-containing seeds are limited. RESULTS: Five polyamine conjugates, including two spermidine and three putrescine conjugates, were tentatively identified in methanolic extracts, using HPLC-DAD-MS. The ratio of putrescine to spermidine conjugates changed with increasing AFB1 concentration in a logistic dose–response manner, with a ratio of below 1 up to a concentration of 51.51 μg kg−1, and approximately 2.54 and 3 at higher concentrations of 177.4 and 308.13 μg kg−1, respectively. The observed variations of the total antioxidant activity and the total phenolic content may support this biphasic behaviour of the seeds against AFB1 stress. CONCLUSIONS: The obtained data are a contribution to the understanding of the roles of polyamine conjugates in seed defence to increasing AFB1 concentrations. According to our knowledge, this study reports for the first time the biphasic response of maize seeds to increasing AFB1 contamination level, comprising the induction of polyamine conjugate accumulation and variation in the ratio of conjugates. This dose–response relationship may provide useful information in the field of agricultural and food chemistry as an indicator of AFB1 contamination level and, hence, for selecting an appropriate seed quality.",
publisher = "Wiley",
journal = "Journal of the Science of Food and Agriculture",
title = "Variations in polyamine conjugates in maize (Zea mays L.) seeds contaminated with aflatoxin B1: a dose–response relationship",
volume = "100",
number = "7",
pages = "2905-2910",
doi = "10.1002/jsfa.10317"
}
Bartolić, D., Maksimović, V., Maksimović, J. D., Stanković, M., Krstović, S., Baošić, R.,& Radotić, K.. (2020). Variations in polyamine conjugates in maize (Zea mays L.) seeds contaminated with aflatoxin B1: a dose–response relationship. in Journal of the Science of Food and Agriculture
Wiley., 100(7), 2905-2910.
https://doi.org/10.1002/jsfa.10317
Bartolić D, Maksimović V, Maksimović JD, Stanković M, Krstović S, Baošić R, Radotić K. Variations in polyamine conjugates in maize (Zea mays L.) seeds contaminated with aflatoxin B1: a dose–response relationship. in Journal of the Science of Food and Agriculture. 2020;100(7):2905-2910.
doi:10.1002/jsfa.10317 .
Bartolić, Dragana, Maksimović, Vuk, Maksimović, Jelena D., Stanković, Mira, Krstović, Saša, Baošić, Rada, Radotić, Ksenija, "Variations in polyamine conjugates in maize (Zea mays L.) seeds contaminated with aflatoxin B1: a dose–response relationship" in Journal of the Science of Food and Agriculture, 100, no. 7 (2020):2905-2910,
https://doi.org/10.1002/jsfa.10317 . .
2
2
2

Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.; Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509

Ilić Đurđić, Karla; Ostafe, Raluca; Đurđević Đelmaš, Aleksandra; Popović, Nikolina; Schillberg, Stefan; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2020)

TY  - DATA
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3836
PB  - Elsevier
T2  - Enzyme and Microbial Technology
T1  - Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509
ER  - 
@misc{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
publisher = "Elsevier",
journal = "Enzyme and Microbial Technology",
title = "Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509"
}
Ilić Đurđić, K., Ostafe, R., Đurđević Đelmaš, A., Popović, N., Schillberg, S., Fischer, R.,& Prodanović, R.. (2020). Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509. in Enzyme and Microbial Technology
Elsevier..
Ilić Đurđić K, Ostafe R, Đurđević Đelmaš A, Popović N, Schillberg S, Fischer R, Prodanović R. Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509. in Enzyme and Microbial Technology. 2020;..
Ilić Đurđić, Karla, Ostafe, Raluca, Đurđević Đelmaš, Aleksandra, Popović, Nikolina, Schillberg, Stefan, Fischer, Rainer, Prodanović, Radivoje, "Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509" in Enzyme and Microbial Technology (2020).

Flow cytometry-based system for screening of lignin peroxidase mutants with higher oxidative stability

Ilić Đurđić, Karla; Ece, Selin; Ostafe, Raluca; Vogel, Simon; Balaž, Ana Marija; Schillberg, Stefan; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2020)

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ece, Selin
AU  - Ostafe, Raluca
AU  - Vogel, Simon
AU  - Balaž, Ana Marija
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3974
AB  - Lignin peroxidase (LiP) is a heme-containing oxidoreductase that oxidizes structurally diverse substrates in an H2O2-dependent manner. Its ability to oxidize many pollutants makes it suitable for bioremediation applications and an ideal candidate for optimization by mutagenesis and selection. In order to increase oxidative stability of LiP we generated a random mutagenesis library comprising 106 mutated LiP genes and screened for expressed enzymes with higher than wild-type activity after incubation in 30 mM H2O2 by flow cytometry with fluorescein-tyramide as a substrate. To preserve the genotype-phenotype connection, the LiP mutants were displayed on the yeast cell surface. Two rounds of sorting were performed, recovered colonies were then screened in microtiter plates, and activity analysis revealed a significant increase in the percentage of cells expressing LiP variants with higher oxidative stability than wtLiP. Two rounds of sorting increased the proportion of more-stable variants from 1.4% in the original library to 52.3%. The most stable variants after two rounds of sorting featured between two and four mutations and retained up to 80% of initial activity after 1 h incubation in 30 mM H2O2. We for the first-time applied flow cytometry for screening of any ligninolytic peroxidase library. Obtained results suggest that developed system may be applied for improvement of industrially important characteristics of lignin peroxidase.
PB  - Elsevier
T2  - Journal of Bioscience and Bioengineering
T1  - Flow cytometry-based system for screening of lignin peroxidase mutants with higher oxidative stability
VL  - 129
IS  - 6
SP  - 664
EP  - 671
DO  - 10.1016/j.jbiosc.2019.12.009
ER  - 
@article{
author = "Ilić Đurđić, Karla and Ece, Selin and Ostafe, Raluca and Vogel, Simon and Balaž, Ana Marija and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Lignin peroxidase (LiP) is a heme-containing oxidoreductase that oxidizes structurally diverse substrates in an H2O2-dependent manner. Its ability to oxidize many pollutants makes it suitable for bioremediation applications and an ideal candidate for optimization by mutagenesis and selection. In order to increase oxidative stability of LiP we generated a random mutagenesis library comprising 106 mutated LiP genes and screened for expressed enzymes with higher than wild-type activity after incubation in 30 mM H2O2 by flow cytometry with fluorescein-tyramide as a substrate. To preserve the genotype-phenotype connection, the LiP mutants were displayed on the yeast cell surface. Two rounds of sorting were performed, recovered colonies were then screened in microtiter plates, and activity analysis revealed a significant increase in the percentage of cells expressing LiP variants with higher oxidative stability than wtLiP. Two rounds of sorting increased the proportion of more-stable variants from 1.4% in the original library to 52.3%. The most stable variants after two rounds of sorting featured between two and four mutations and retained up to 80% of initial activity after 1 h incubation in 30 mM H2O2. We for the first-time applied flow cytometry for screening of any ligninolytic peroxidase library. Obtained results suggest that developed system may be applied for improvement of industrially important characteristics of lignin peroxidase.",
publisher = "Elsevier",
journal = "Journal of Bioscience and Bioengineering",
title = "Flow cytometry-based system for screening of lignin peroxidase mutants with higher oxidative stability",
volume = "129",
number = "6",
pages = "664-671",
doi = "10.1016/j.jbiosc.2019.12.009"
}
Ilić Đurđić, K., Ece, S., Ostafe, R., Vogel, S., Balaž, A. M., Schillberg, S., Fischer, R.,& Prodanović, R.. (2020). Flow cytometry-based system for screening of lignin peroxidase mutants with higher oxidative stability. in Journal of Bioscience and Bioengineering
Elsevier., 129(6), 664-671.
https://doi.org/10.1016/j.jbiosc.2019.12.009
Ilić Đurđić K, Ece S, Ostafe R, Vogel S, Balaž AM, Schillberg S, Fischer R, Prodanović R. Flow cytometry-based system for screening of lignin peroxidase mutants with higher oxidative stability. in Journal of Bioscience and Bioengineering. 2020;129(6):664-671.
doi:10.1016/j.jbiosc.2019.12.009 .
Ilić Đurđić, Karla, Ece, Selin, Ostafe, Raluca, Vogel, Simon, Balaž, Ana Marija, Schillberg, Stefan, Fischer, Rainer, Prodanović, Radivoje, "Flow cytometry-based system for screening of lignin peroxidase mutants with higher oxidative stability" in Journal of Bioscience and Bioengineering, 129, no. 6 (2020):664-671,
https://doi.org/10.1016/j.jbiosc.2019.12.009 . .
4
1
2

Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide

Balaž, Ana Marija; Stevanović, Jelena; Ostafe, Raluca; Blazić, Marija; Ilić Đurđić, Karla; Fischer, Rainer; Prodanović, Radivoje

(2020)

TY  - JOUR
AU  - Balaž, Ana Marija
AU  - Stevanović, Jelena
AU  - Ostafe, Raluca
AU  - Blazić, Marija
AU  - Ilić Đurđić, Karla
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4011
AB  - Cellobiose dehydrogenase (CDH, EC 1.1.99.18) from white rot fungi Phanerochaete chrysosporium can be used for constructing biosensors and biofuel cells, for bleaching cotton in textile industry, and recently, the enzyme has found an important application in biomedicine as an antimicrobial and antibiofilm agent. Stability and activity of the wild-type (wt) CDH and mutants at methionine residues in the presence of hydrogen peroxide were investigated. Saturation mutagenesis libraries were made at the only methionine in heme domain M65 and two methionines M685 and M738 in the flavin domain that were closest to the active site. After screening the libraries, three mutants with increased activity and stability in the presence of peroxide were found, M65F with 70% of residual activity after 6 h of incubation in 0.3 M hydrogen peroxide, M738S with 80% of residual activity and M685Y with over 90% of residual activity compared to wild-type CDH that retained 40% of original activity. Combined mutants showed no activity. The most stable mutant M685Y with 5.8 times increased half-life in the presence of peroxide showed also 2.5 times increased kcat for lactose compared to wtCDH and could be good candidate for applications in biofuel cells and biocatalysis for lactobionic acid production.
T2  - Molecular Diversity
T1  - Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide
VL  - 24
IS  - 3
SP  - 593
EP  - 601
DO  - 10.1007/s11030-019-09965-0
ER  - 
@article{
author = "Balaž, Ana Marija and Stevanović, Jelena and Ostafe, Raluca and Blazić, Marija and Ilić Đurđić, Karla and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Cellobiose dehydrogenase (CDH, EC 1.1.99.18) from white rot fungi Phanerochaete chrysosporium can be used for constructing biosensors and biofuel cells, for bleaching cotton in textile industry, and recently, the enzyme has found an important application in biomedicine as an antimicrobial and antibiofilm agent. Stability and activity of the wild-type (wt) CDH and mutants at methionine residues in the presence of hydrogen peroxide were investigated. Saturation mutagenesis libraries were made at the only methionine in heme domain M65 and two methionines M685 and M738 in the flavin domain that were closest to the active site. After screening the libraries, three mutants with increased activity and stability in the presence of peroxide were found, M65F with 70% of residual activity after 6 h of incubation in 0.3 M hydrogen peroxide, M738S with 80% of residual activity and M685Y with over 90% of residual activity compared to wild-type CDH that retained 40% of original activity. Combined mutants showed no activity. The most stable mutant M685Y with 5.8 times increased half-life in the presence of peroxide showed also 2.5 times increased kcat for lactose compared to wtCDH and could be good candidate for applications in biofuel cells and biocatalysis for lactobionic acid production.",
journal = "Molecular Diversity",
title = "Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide",
volume = "24",
number = "3",
pages = "593-601",
doi = "10.1007/s11030-019-09965-0"
}
Balaž, A. M., Stevanović, J., Ostafe, R., Blazić, M., Ilić Đurđić, K., Fischer, R.,& Prodanović, R.. (2020). Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide. in Molecular Diversity, 24(3), 593-601.
https://doi.org/10.1007/s11030-019-09965-0
Balaž AM, Stevanović J, Ostafe R, Blazić M, Ilić Đurđić K, Fischer R, Prodanović R. Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide. in Molecular Diversity. 2020;24(3):593-601.
doi:10.1007/s11030-019-09965-0 .
Balaž, Ana Marija, Stevanović, Jelena, Ostafe, Raluca, Blazić, Marija, Ilić Đurđić, Karla, Fischer, Rainer, Prodanović, Radivoje, "Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide" in Molecular Diversity, 24, no. 3 (2020):593-601,
https://doi.org/10.1007/s11030-019-09965-0 . .
5
2
3

Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain

Balaž, Ana Marija; Blažić, Marija; Popović, Nikolina; Prodanović, Olivera; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(Belgrade : Serbian Chemical Society, 2020)

TY  - JOUR
AU  - Balaž, Ana Marija
AU  - Blažić, Marija
AU  - Popović, Nikolina
AU  - Prodanović, Olivera
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4270
AB  - Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZα plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion- -exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s-1 for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM-1 s-1. All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture.
AB  - У циљу употребе у биосензорима и биогоривним ћелијама, успостављена је производњарастворних облика целобиоза дехидрогеназе (CDH) претходно еволуираних на површиниквашчевих ћелија S. cerevisiae. У ту сврху су мутанти CDH, tm (D20N, A64T, V592M), H5(D20N, V22A, A64T, V592M) и H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S)клонирани у pPICZα плазмид и трансформисани у Pichia pastoris KM71H сој за високуекспресију у растворном облику и кинетичку карактеризацију. После 6 дана експресије подиндукцијом метанолом, мутанти су пречишћени ултрафилтрацијом, јоноизмењивачкомхроматографијом и гел-филтрацијом. SDS електрофореза је потврдила чистоћу уз присуствоједне протеинске траке молекулскe масe од 100 kDa. Кинетичка карактеризација је показалада H5 мутирани протеин поседује највећу каталитичку константу од 43,5 s-1 за лактозу, докје H9 имао највећу константу специфичности за лактозу од 132 mM-1 s-1. Сва три мутиранапротеина су имала неизмењен pH оптимум који је био у опсегу од 4,5 до 5,5. У поређењу сапретходно добијеним природним и мутантним облицима CDH протеина из Phanerochaetechrysosporium, облици приказани у овом раду имају већу активност и специфичност, што их,повезано са високом експресијом протеина у P. Pastoris, чини добрим кандидатима за упо-требу у биотехнологији за производњу лактобионске киселине и биосензора.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain
T1  - Ekspresija, prečišćavanje i karakterizacija mutanata celobioza - dehidrogenaze iz Phanerochaete chrysosporium u Pichia pastoris KM71H soju
VL  - 85
IS  - 1
SP  - 25
EP  - 35
DO  - 10.2298/JSC190320058B
ER  - 
@article{
author = "Balaž, Ana Marija and Blažić, Marija and Popović, Nikolina and Prodanović, Olivera and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
abstract = "Production of soluble cellobiose dehydrogenase (CDH) mutant proteins previously evolved on the surface of S. cerevisiae yeast cells was established for use in biosensors and biofuel cells. For this purpose, mutant cdh genes tm (D20N, A64T, V592M), H5 (D20N, V22A, A64T, V592M) and H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S) were cloned to pPICZα plasmid and transformed into Pichia pastoris KM71H strain for high expression in a soluble form and kinetic characterization. After 6 days of expression under methanol induction, the CDHs were purified by ultrafiltration, ion- -exchange chromatography and gel filtration. Sodium dodecyl sulfate electrophoresis confirmed the purity and presence of a single protein band at a molecular weight of 100 kDa. Kinetic characterization showed that the H5 mutant had the highest catalytic constant of 43.5 s-1 for lactose, while the mutant H9 showed the highest specificity constant for lactose of 132 mM-1 s-1. All three mutant proteins did not change the pH optimum that was between 4.5 and 5.5. Compared to the previously obtained wild types and mutants of CDH from Phanerochaete chrysosporium, the variants reported in this article had higher activity and specificity that together with high protein expression rate in P. pastoris, makes them good candidates for use in biotechnology for lactobionic acid production and biosensor manufacture., У циљу употребе у биосензорима и биогоривним ћелијама, успостављена је производњарастворних облика целобиоза дехидрогеназе (CDH) претходно еволуираних на површиниквашчевих ћелија S. cerevisiae. У ту сврху су мутанти CDH, tm (D20N, A64T, V592M), H5(D20N, V22A, A64T, V592M) и H9 (D20N, A64T, T84A, A261P, V592M, E674G, N715S)клонирани у pPICZα плазмид и трансформисани у Pichia pastoris KM71H сој за високуекспресију у растворном облику и кинетичку карактеризацију. После 6 дана експресије подиндукцијом метанолом, мутанти су пречишћени ултрафилтрацијом, јоноизмењивачкомхроматографијом и гел-филтрацијом. SDS електрофореза је потврдила чистоћу уз присуствоједне протеинске траке молекулскe масe од 100 kDa. Кинетичка карактеризација је показалада H5 мутирани протеин поседује највећу каталитичку константу од 43,5 s-1 за лактозу, докје H9 имао највећу константу специфичности за лактозу од 132 mM-1 s-1. Сва три мутиранапротеина су имала неизмењен pH оптимум који је био у опсегу од 4,5 до 5,5. У поређењу сапретходно добијеним природним и мутантним облицима CDH протеина из Phanerochaetechrysosporium, облици приказани у овом раду имају већу активност и специфичност, што их,повезано са високом експресијом протеина у P. Pastoris, чини добрим кандидатима за упо-требу у биотехнологији за производњу лактобионске киселине и биосензора.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain, Ekspresija, prečišćavanje i karakterizacija mutanata celobioza - dehidrogenaze iz Phanerochaete chrysosporium u Pichia pastoris KM71H soju",
volume = "85",
number = "1",
pages = "25-35",
doi = "10.2298/JSC190320058B"
}
Balaž, A. M., Blažić, M., Popović, N., Prodanović, O., Ostafe, R., Fischer, R.,& Prodanović, R.. (2020). Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 85(1), 25-35.
https://doi.org/10.2298/JSC190320058B
Balaž AM, Blažić M, Popović N, Prodanović O, Ostafe R, Fischer R, Prodanović R. Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain. in Journal of the Serbian Chemical Society. 2020;85(1):25-35.
doi:10.2298/JSC190320058B .
Balaž, Ana Marija, Blažić, Marija, Popović, Nikolina, Prodanović, Olivera, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Expression, purification and characterization of cellobiose dehydrogenase mutants from Phanerochaete chrysosporium in Pichia pastoris KM71H strain" in Journal of the Serbian Chemical Society, 85, no. 1 (2020):25-35,
https://doi.org/10.2298/JSC190320058B . .

Ispitivanje koordinativnih sposobnosti epinefrina prema Fe2+ i Fe3+ katjonima i redoks aktivnost nastalih kompleksa

Korać Jačić, Jelena K.

(Универзитет у Београду, Хемијски факултет, 2020)

TY  - THES
AU  - Korać Jačić, Jelena K.
PY  - 2020
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7870
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:23173/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=31031049
UR  - https://nardus.mpn.gov.rs/handle/123456789/17801
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4365
AB  - Epinefrin je kateholamin sa značajnom fiziološkom ulogom. Konformacija ovog molekulautiče na njegovu interakciju sa drugim molekulima i na njegove biološke efekte. Na fiziološkimpH vrednostima, koordinativne sposobnosti epinefrina prema gvožđu i redoks interakcije epinefrinasa gvožđem su od suštinske važnosti za razumevanje dve veoma različite pojave. Prva pojava ještetno dejstvo koje hronični psihološki/sredinski stres izaziva na nivou kardiovaskularnog sistema.Druga pojava je umrežavanje kateholaminima bogatih biopolimera i struktura. Kako bi se rasvetlileuloge rastvarača i vodoničnih veza u interakcijama epinefrina sa gvožđem, proučavana jekonformacija epinefrina u vodi i polarnom rastvaraču dimetil sulfoksidu (DMSO).U ovoj disertaciji su predstavljeni rezultati proučavanja mehanizama interakcije epinefrinasa Fe2+ i Fe3+ jonima pri različitim koncentracionim odnosima na pH 7,4, odnosno na pH vrednostikoja odgovara fiziološkim uslovima. U svrhu istraživanja bioloških efekata epinefrina, u ovojdisertaciji su predstavljena ispitivanja efekta Epi-Fe3+ kompleksa na ćelije koje konstitutivnoeksprimiraju adrenergičke receptore.Konformacije epinefrina u polarnim rastvaračima, vodi i DMSO, su proučavane metodamaH nuklearne magnetne rezonance (1H NMR) kao i dvodimenzionalnim metodama nuklearnemagnetne rezonance, i to: 1H - 1H COSY, 1H - 15N HSQC i NOESY. Na NH2 i CH2 grupamaepinefrina su uočeni hemijski neekvivalentni protoni prilikom korišćenja DMSO kao rastvarača.Ove pojave nisu uočene kada je rastvarač bila voda. Analizom uticaja korišćenog rastvarača naNMR spektar, i analizom uticaja povećanja temperature uzorka na NMR spektar, dolazi se dozaključka da jedan od protona amino grupe formira jaku intramolekulsku vezu sa alifatičnomhidroksilnom grupom, koja je pak H donor drugoj intermolekularnoj vezi sa DMSO. PomoćuNOESY metode su prikupljeni podaci o prostornoj poziciji protona u bočnom lancu. Na taj način jeformiran 3D model konformacije epinefrina u DMSO. Ukratko, epinefrin formira dodatni petočlaniprsten koji sadrži bifurkovane intramolekulske/intermolekulske vodonične veze i zauzima strukturuoblika škorpiona, gde kateholni prsten predstavlja telo škorpiona, a bočni lanac predstavlja rep kojije povijen u smeru glave škorpiona. U vodi, kao rastvaraču, konformacija epinefrina ne posedujeintramolekulske vodonične veze pa je tada struktura ovog molekula najverovatnije definisanavodoničnim vezama sa molekulima vode.U okviru ove disertacije ispitivanjima je ustanovljeno da epinefrin sa Fe3+ jonima gradistabilne visokospinske komplekse čija je stehiometrija 1:1 ili 3:1. Stehiometrija ovog kompleksazavisi od odnosa koncentracija epinefrina i Fe3+ jona. Na kateholnom prstenu epinefrina atomikiseonika predstavljaju mesto za formiranje koordinacione veze unutar fiziološki relevantnogbidentatnog 1:1 kompleksa. Fe3+ katjon ima slab uticaj na redoks osobine epinefrina. Međutim,epinefrin i Fe2+ joni grade kompleks koji je jak redukcioni agens. Posledica je redukcija O2,proizvodnja vodonik peroksida i formiranje Epi-Fe3+ kompleksa. U ovom procesu epinefrin se neoksiduje, odnosno Fe2+ jon nije prenosilac, već donor elektrona. Oksidacija Fe2+ jona koja jekatalizovana epinefrinom predstavlja moguće hemijsko objašnjenje za stresom izazvana oštećenjaćelija srca. Takođe, rezultati ovih ispitivanja su u skladu sa prethodnim istraživanjima kateholaminau polimerima i njihovih interakcija sa gvožđem, i upućuju na nove strategije za poboljšavanjeefikasnosti umrežavanja kateholaminima bogatih biopolimera i struktura.U stresnim situacijama epinefrin se luči i može interagovati sa labilnim gvožđem koje senalazi u ljudskoj plazmi. Te interakcije mogu prouzrokovati značajne patofiziološke posledice. Uivovoj disertaciji su prikazani rezultati istraživanja prema kojima epinefrin i Fe3+ joni na fiziološkompH grade stabilni 1:1 bidentatni kompleks. Takođe je pokazano da na fiziološkom pH epinefrin nedegradira u prisustvu gvožđa. Utvrđeno je i da epinefrin i Fe2+ joni grade bezbojni kompleks i da jetaj kompleks stabilan pri anaerobnim uslovima. Uočeno je i da epinefrin u prisustvu O2 značajnopromoviše oksidaciju Fe2+ jona i formiranje Epi-Fe3+ kompleksa. Pri eksperimentima rađenimmetodom ciklične voltametrije, Epi-Fe2+ kompleks je pokazao potencijal E1/2 = -582 mV (u odnosuna standardnu vodoničnu elektrodu). Ovakva vrednost E1/2 potencijala objašnjava katalizovanuoksidaciju. Interakcije sa gvožđem mogu uticati na biološke efekte/efikasnost epinefrina. Uticajvezivanja gvožđa na biološko ponašanje epinefrina je ispitivan metodom nametnute voltaže nadeliću membrane u konfiguraciji cela ćelija, u kulturi ćelija koje konstitutivno eksprimirajuadrenergičke receptore. Epinefrin je samostalno, bez značajnog prisustva gvožđa, uzrokovaopovećanje amplitude struja usmerenih ka spoljašnosti ćelija, tj. povećanje izlaznih struja. Kompleksepinefrina sa Fe3+ nije izazivao slične posledice. Ovim se nameće zaključak da formiranjekompleksa sa gvožđem sprečava vezivanje epinefrina za adrenergičke receptore i njihovuposledičnu aktivaciju. Prooksidativna aktivnost Epi-Fe2+ kompleksa možda predstavlja vezu izmeđuhroničnog stresa i kardiovaskularnih problema, a labilno gvožđe u plazmi je potencijalni modulatorbioloških aktivnosti liganda.
AB  - Epinephrine (Epi) is a catecholamine with important physiological roles. Interactions withother molecules and associated biological effects of Epi are controlled by its molecularconformation. Coordinate interactions of epinephrine with iron at physiological pH and their redoxactivity are crucial for understanding two distinct phenomena. First, the adverse effects that chronicstress causes to cardiovascular system. Second, the cross-linking of biopolymers and frameworkswhich are rich in catecholamines. Conformation of epinephrine in polar solvents, namely indimethyl sulfoxide (DMSO) and water, was investigated in order to shed light on effects solventsand hydrogen bonds exert on interactions of epinephrine with iron.Mechanism of epinephrine interactions with Fe2+ and Fe3+ ions was studied at differentconcentration ratios, at physiological pH (pH 7.4), and the results are presented in this dissertation.For the sake of exploration of biological effects of epinephrine, this dissertation also contains theresults of examination of effects Epi-Fe3+ complex has on cell culture with constitutive expressionof adrenergic receptors.Conformation of epinephrine in polar solvents, namely in dimethyl sulfoxide (DMSO) andwater, was investigated using 1H NMR, 1H - 1H COSY, NOESY and 1H - 15N HSQC methods.When DMSO was used as a solvent, chemical and magnetic nonequivalence of protons was spottedat NH2 and CH2 groups on epinephrine. Characteristics of hydrogen bonds in DMSO weredetermined by studying effect which temperature rise has on NMR spectra and also analyzinginfluences of solvent substitution on NMR spectra. Results have shown that epinephrine inducesstrong intramolecular bond between one of the protons of NH2 group and the OH group on the sidechain. On the other hand, the OH group on the side chain, i.e. the aliphatic OH group, presents aproton donor for intermolecular bond between epinephrine and DMSO. This phenomenon was notnoticed when water was used as a solvent. 3D modelling of epinephrine molecule structure wasbased on information about spatial arrangement of protons, which in turn was obtained usingNOESY method. Obtained 3D model shows that epinephrine in DMSO has a rigid structure thatresembles the shape of a scorpion, in which the catechol ring presents the body of the scorpion andthe side chain presents the tail of the scorpion. This structure is a consequence of formation of anadditional five–membered ring limited by inter/intra–molecular bonds. If water is used as a solvent(instead of DMSO), epinephrine takes different and non-rigid conformation which does not possessthe aforementioned intramolecular hydrogen bond. In this case, conformation of epinephrine isdetermined by hydrogen bonds with solvent molecules.Examinations conducted in the scope of this dissertation showed that epinephrine and Fe3+form stable high-spin complexes in 1:1 and 3:1 stoichiometry. Stoichiometry of these depends onconcentration ratio of epinephrine and Fe3+. Results acquired using Raman spectroscopy haveshown that 1:1 bidentate Epi–Fe3+ complex is formed by coordinative bonding of Fe3+ ions toepinephrine molecule through O atoms on the catechol ring. Effect of Fe3+ and Fe2+ ions on redoxproperties of epinephrine was studied using method of cyclic voltammetry. It was observed thatFe3+ ions do not significantly affect redox properties of epinephrine, but epinephrine with Fe2+ ionsforms strong reducing agent. Fe2+ ion presents electron donor that in the presence of epinephrinereduces O2 and causes production of H2O2. Specific hemism of epinephrine, which includesoxidation of Fe2+ ions, may present a mechanism that explains stress-induced cardiotoxicity andheart diseases. Also, these results can be used for improvement of synthesis and development ofbiopolymers.viIn stressful situations epinephrine is released and it may interact with labile iron in humanblood plasma. These interactions can have potentially important (patho)physiological effects. In thisdissertation, it is shown that at physiological pH epinephrine and Fe3+ build stable 1:1 high-spinbidentate complex. It is also shown that in presence of iron, at physiological pH, epinephrine doesnot degrade. It was observed that epinephrine and Fe2+ build colorless complex, which was stableunder anaerobic conditions. In presence of O2, epinephrine significantly catalyzed oxidation of Fe2+ions and formation of Epi-Fe3+ complex. Cyclic voltammetry results showed that the mid-pointpotential of Epi-Fe2+ complex equals -582 mV (vs. standard hydrogen electrode). This value ofmid-point potential explains the oxidation promotion. Biological effects/efficiency of epinephrineare influenced by its interaction with iron. Iron binding effects on biological performance ofepinephrine were examined using patch clamping in cell culture with constitutive expression ofadrenergic receptors. Epinephrine, on its own, induced an increase of outward currents, whereasEpi-Fe3+ complex did not evoke similar phenomenon. These imply that the binding of epinephrineto adrenergic receptors and their activation is inhibited by the formation of the complex of Epi withiron. Oxidative promoting activity of Fe2+ in the presence epinephrine may represent a basis forcardiovascular problems caused by chronic stress. The results obtained in this dissertation indicatethat the labile iron pool may have a new function that represents a modulation of the activity ofbiologically significant ligands/molecules.Epinephrine (Epi) is a catecholamine with important physiological roles. Interactions withother molecules and associated biological effects of Epi are controlled by its molecularconformation. Coordinate interactions of epinephrine with iron at physiological pH and their redoxactivity are crucial for understanding two distinct phenomena. First, the adverse effects that chronicstress causes to cardiovascular system. Second, the cross-linking of biopolymers and frameworkswhich are rich in catecholamines. Conformation of epinephrine in polar solvents, namely indimethyl sulfoxide (DMSO) and water, was investigated in order to shed light on effects solventsand hydrogen bonds exert on interactions of epinephrine with iron.Mechanism of epinephrine interactions with Fe2+ and Fe3+ ions was studied at differentconcentration ratios, at physiological pH (pH 7.4), and the results are presented in this dissertation.For the sake of exploration of biological effects of epinephrine, this dissertation also contains theresults of examination of effects Epi-Fe3+ complex has on cell culture with constitutive expressionof adrenergic receptors.Conformation of epinephrine in polar solvents, namely in dimethyl sulfoxide (DMSO) andwater, was investigated using 1H NMR, 1H - 1H COSY, NOESY and 1H - 15N HSQC methods.When DMSO was used as a solvent, chemical and magnetic nonequivalence of protons was spottedat NH2 and CH2 groups on epinephrine. Characteristics of hydrogen bonds in DMSO weredetermined by studying effect which temperature rise has on NMR spectra and also analyzinginfluences of solvent substitution on NMR spectra. Results have shown that epinephrine inducesstrong intramolecular bond between one of the protons of NH2 group and the OH group on the sidechain. On the other hand, the OH group on the side chain, i.e. the aliphatic OH group, presents aproton donor for intermolecular bond between epinephrine and DMSO. This phenomenon was notnoticed when water was used as a solvent. 3D modelling of epinephrine molecule structure wasbased on information about spatial arrangement of protons, which in turn was obtained usingNOESY method. Obtained 3D model shows that epinephrine in DMSO has a rigid structure thatresembles the shape of a scorpion, in which the catechol ring presents the body of the scorpion andthe side chain presents the tail of the scorpion. This structure is a consequence of formation of anadditional five–membered ring limited by inter/intra–molecular bonds. If water is used as a solvent(instead of DMSO), epinephrine takes different and non-rigid conformation which does not possessthe aforementioned intramolecular hydrogen bond. In this case, conformation of epinephrine isdetermined by hydrogen bonds with solvent molecules.Examinations conducted in the scope of this dissertation showed that epinephrine and Fe3+form stable high-spin complexes in 1:1 and 3:1 stoichiometry. Stoichiometry of these depends onconcentration ratio of epinephrine and Fe3+. Results acquired using Raman spectroscopy haveshown that 1:1 bidentate Epi–Fe3+ complex is formed by coordinative bonding of Fe3+ ions toepinephrine molecule through O atoms on the catechol ring. Effect of Fe3+ and Fe2+ ions on redoxproperties of epinephrine was studied using method of cyclic voltammetry. It was observed thatFe3+ ions do not significantly affect redox properties of epinephrine, but epinephrine with Fe2+ ionsforms strong reducing agent. Fe2+ ion presents electron donor that in the presence of epinephrinereduces O2 and causes production of H2O2. Specific hemism of epinephrine, which includesoxidation of Fe2+ ions, may present a mechanism that explains stress-induced cardiotoxicity andheart diseases. Also, these results can be used for improvement of synthesis and development ofbiopolymers.viIn stressful situations epinephrine is released and it may interact with labile iron in humanblood plasma. These interactions can have potentially important (patho)physiological effects. In thisdissertation, it is shown that at physiological pH epinephrine and Fe3+ build stable 1:1 high-spinbidentate complex. It is also shown that in presence of iron, at physiological pH, epinephrine doesnot degrade. It was observed that epinephrine and Fe2+ build colorless complex, which was stableunder anaerobic conditions. In presence of O2, epinephrine significantly catalyzed oxidation of Fe2+ions and formation of Epi-Fe3+ complex. Cyclic voltammetry results showed that the mid-pointpotential of Epi-Fe2+ complex equals -582 mV (vs. standard hydrogen electrode). This value ofmid-point potential explains the oxidation promotion. Biological effects/efficiency of epinephrineare influenced by its interaction with iron. Iron binding effects on biological performance ofepinephrine were examined using patch clamping in cell culture with constitutive expression ofadrenergic receptors. Epinephrine, on its own, induced an increase of outward currents, whereasEpi-Fe3+ complex did not evoke similar phenomenon. These imply that the binding of epinephrineto adrenergic receptors and their activation is inhibited by the formation of the complex of Epi withiron. Oxidative promoting activity of Fe2+ in the presence epinephrine may represent a basis forcardiovascular problems caused by chronic stress. The results obtained in this dissertation indicatethat the labile iron pool may have a new function that represents a modulation of the activity ofbiologically significant ligands/molecules.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Ispitivanje koordinativnih sposobnosti epinefrina prema Fe2+ i Fe3+ katjonima i redoks aktivnost nastalih kompleksa
ER  - 
@phdthesis{
author = "Korać Jačić, Jelena K.",
year = "2020",
abstract = "Epinefrin je kateholamin sa značajnom fiziološkom ulogom. Konformacija ovog molekulautiče na njegovu interakciju sa drugim molekulima i na njegove biološke efekte. Na fiziološkimpH vrednostima, koordinativne sposobnosti epinefrina prema gvožđu i redoks interakcije epinefrinasa gvožđem su od suštinske važnosti za razumevanje dve veoma različite pojave. Prva pojava ještetno dejstvo koje hronični psihološki/sredinski stres izaziva na nivou kardiovaskularnog sistema.Druga pojava je umrežavanje kateholaminima bogatih biopolimera i struktura. Kako bi se rasvetlileuloge rastvarača i vodoničnih veza u interakcijama epinefrina sa gvožđem, proučavana jekonformacija epinefrina u vodi i polarnom rastvaraču dimetil sulfoksidu (DMSO).U ovoj disertaciji su predstavljeni rezultati proučavanja mehanizama interakcije epinefrinasa Fe2+ i Fe3+ jonima pri različitim koncentracionim odnosima na pH 7,4, odnosno na pH vrednostikoja odgovara fiziološkim uslovima. U svrhu istraživanja bioloških efekata epinefrina, u ovojdisertaciji su predstavljena ispitivanja efekta Epi-Fe3+ kompleksa na ćelije koje konstitutivnoeksprimiraju adrenergičke receptore.Konformacije epinefrina u polarnim rastvaračima, vodi i DMSO, su proučavane metodamaH nuklearne magnetne rezonance (1H NMR) kao i dvodimenzionalnim metodama nuklearnemagnetne rezonance, i to: 1H - 1H COSY, 1H - 15N HSQC i NOESY. Na NH2 i CH2 grupamaepinefrina su uočeni hemijski neekvivalentni protoni prilikom korišćenja DMSO kao rastvarača.Ove pojave nisu uočene kada je rastvarač bila voda. Analizom uticaja korišćenog rastvarača naNMR spektar, i analizom uticaja povećanja temperature uzorka na NMR spektar, dolazi se dozaključka da jedan od protona amino grupe formira jaku intramolekulsku vezu sa alifatičnomhidroksilnom grupom, koja je pak H donor drugoj intermolekularnoj vezi sa DMSO. PomoćuNOESY metode su prikupljeni podaci o prostornoj poziciji protona u bočnom lancu. Na taj način jeformiran 3D model konformacije epinefrina u DMSO. Ukratko, epinefrin formira dodatni petočlaniprsten koji sadrži bifurkovane intramolekulske/intermolekulske vodonične veze i zauzima strukturuoblika škorpiona, gde kateholni prsten predstavlja telo škorpiona, a bočni lanac predstavlja rep kojije povijen u smeru glave škorpiona. U vodi, kao rastvaraču, konformacija epinefrina ne posedujeintramolekulske vodonične veze pa je tada struktura ovog molekula najverovatnije definisanavodoničnim vezama sa molekulima vode.U okviru ove disertacije ispitivanjima je ustanovljeno da epinefrin sa Fe3+ jonima gradistabilne visokospinske komplekse čija je stehiometrija 1:1 ili 3:1. Stehiometrija ovog kompleksazavisi od odnosa koncentracija epinefrina i Fe3+ jona. Na kateholnom prstenu epinefrina atomikiseonika predstavljaju mesto za formiranje koordinacione veze unutar fiziološki relevantnogbidentatnog 1:1 kompleksa. Fe3+ katjon ima slab uticaj na redoks osobine epinefrina. Međutim,epinefrin i Fe2+ joni grade kompleks koji je jak redukcioni agens. Posledica je redukcija O2,proizvodnja vodonik peroksida i formiranje Epi-Fe3+ kompleksa. U ovom procesu epinefrin se neoksiduje, odnosno Fe2+ jon nije prenosilac, već donor elektrona. Oksidacija Fe2+ jona koja jekatalizovana epinefrinom predstavlja moguće hemijsko objašnjenje za stresom izazvana oštećenjaćelija srca. Takođe, rezultati ovih ispitivanja su u skladu sa prethodnim istraživanjima kateholaminau polimerima i njihovih interakcija sa gvožđem, i upućuju na nove strategije za poboljšavanjeefikasnosti umrežavanja kateholaminima bogatih biopolimera i struktura.U stresnim situacijama epinefrin se luči i može interagovati sa labilnim gvožđem koje senalazi u ljudskoj plazmi. Te interakcije mogu prouzrokovati značajne patofiziološke posledice. Uivovoj disertaciji su prikazani rezultati istraživanja prema kojima epinefrin i Fe3+ joni na fiziološkompH grade stabilni 1:1 bidentatni kompleks. Takođe je pokazano da na fiziološkom pH epinefrin nedegradira u prisustvu gvožđa. Utvrđeno je i da epinefrin i Fe2+ joni grade bezbojni kompleks i da jetaj kompleks stabilan pri anaerobnim uslovima. Uočeno je i da epinefrin u prisustvu O2 značajnopromoviše oksidaciju Fe2+ jona i formiranje Epi-Fe3+ kompleksa. Pri eksperimentima rađenimmetodom ciklične voltametrije, Epi-Fe2+ kompleks je pokazao potencijal E1/2 = -582 mV (u odnosuna standardnu vodoničnu elektrodu). Ovakva vrednost E1/2 potencijala objašnjava katalizovanuoksidaciju. Interakcije sa gvožđem mogu uticati na biološke efekte/efikasnost epinefrina. Uticajvezivanja gvožđa na biološko ponašanje epinefrina je ispitivan metodom nametnute voltaže nadeliću membrane u konfiguraciji cela ćelija, u kulturi ćelija koje konstitutivno eksprimirajuadrenergičke receptore. Epinefrin je samostalno, bez značajnog prisustva gvožđa, uzrokovaopovećanje amplitude struja usmerenih ka spoljašnosti ćelija, tj. povećanje izlaznih struja. Kompleksepinefrina sa Fe3+ nije izazivao slične posledice. Ovim se nameće zaključak da formiranjekompleksa sa gvožđem sprečava vezivanje epinefrina za adrenergičke receptore i njihovuposledičnu aktivaciju. Prooksidativna aktivnost Epi-Fe2+ kompleksa možda predstavlja vezu izmeđuhroničnog stresa i kardiovaskularnih problema, a labilno gvožđe u plazmi je potencijalni modulatorbioloških aktivnosti liganda., Epinephrine (Epi) is a catecholamine with important physiological roles. Interactions withother molecules and associated biological effects of Epi are controlled by its molecularconformation. Coordinate interactions of epinephrine with iron at physiological pH and their redoxactivity are crucial for understanding two distinct phenomena. First, the adverse effects that chronicstress causes to cardiovascular system. Second, the cross-linking of biopolymers and frameworkswhich are rich in catecholamines. Conformation of epinephrine in polar solvents, namely indimethyl sulfoxide (DMSO) and water, was investigated in order to shed light on effects solventsand hydrogen bonds exert on interactions of epinephrine with iron.Mechanism of epinephrine interactions with Fe2+ and Fe3+ ions was studied at differentconcentration ratios, at physiological pH (pH 7.4), and the results are presented in this dissertation.For the sake of exploration of biological effects of epinephrine, this dissertation also contains theresults of examination of effects Epi-Fe3+ complex has on cell culture with constitutive expressionof adrenergic receptors.Conformation of epinephrine in polar solvents, namely in dimethyl sulfoxide (DMSO) andwater, was investigated using 1H NMR, 1H - 1H COSY, NOESY and 1H - 15N HSQC methods.When DMSO was used as a solvent, chemical and magnetic nonequivalence of protons was spottedat NH2 and CH2 groups on epinephrine. Characteristics of hydrogen bonds in DMSO weredetermined by studying effect which temperature rise has on NMR spectra and also analyzinginfluences of solvent substitution on NMR spectra. Results have shown that epinephrine inducesstrong intramolecular bond between one of the protons of NH2 group and the OH group on the sidechain. On the other hand, the OH group on the side chain, i.e. the aliphatic OH group, presents aproton donor for intermolecular bond between epinephrine and DMSO. This phenomenon was notnoticed when water was used as a solvent. 3D modelling of epinephrine molecule structure wasbased on information about spatial arrangement of protons, which in turn was obtained usingNOESY method. Obtained 3D model shows that epinephrine in DMSO has a rigid structure thatresembles the shape of a scorpion, in which the catechol ring presents the body of the scorpion andthe side chain presents the tail of the scorpion. This structure is a consequence of formation of anadditional five–membered ring limited by inter/intra–molecular bonds. If water is used as a solvent(instead of DMSO), epinephrine takes different and non-rigid conformation which does not possessthe aforementioned intramolecular hydrogen bond. In this case, conformation of epinephrine isdetermined by hydrogen bonds with solvent molecules.Examinations conducted in the scope of this dissertation showed that epinephrine and Fe3+form stable high-spin complexes in 1:1 and 3:1 stoichiometry. Stoichiometry of these depends onconcentration ratio of epinephrine and Fe3+. Results acquired using Raman spectroscopy haveshown that 1:1 bidentate Epi–Fe3+ complex is formed by coordinative bonding of Fe3+ ions toepinephrine molecule through O atoms on the catechol ring. Effect of Fe3+ and Fe2+ ions on redoxproperties of epinephrine was studied using method of cyclic voltammetry. It was observed thatFe3+ ions do not significantly affect redox properties of epinephrine, but epinephrine with Fe2+ ionsforms strong reducing agent. Fe2+ ion presents electron donor that in the presence of epinephrinereduces O2 and causes production of H2O2. Specific hemism of epinephrine, which includesoxidation of Fe2+ ions, may present a mechanism that explains stress-induced cardiotoxicity andheart diseases. Also, these results can be used for improvement of synthesis and development ofbiopolymers.viIn stressful situations epinephrine is released and it may interact with labile iron in humanblood plasma. These interactions can have potentially important (patho)physiological effects. In thisdissertation, it is shown that at physiological pH epinephrine and Fe3+ build stable 1:1 high-spinbidentate complex. It is also shown that in presence of iron, at physiological pH, epinephrine doesnot degrade. It was observed that epinephrine and Fe2+ build colorless complex, which was stableunder anaerobic conditions. In presence of O2, epinephrine significantly catalyzed oxidation of Fe2+ions and formation of Epi-Fe3+ complex. Cyclic voltammetry results showed that the mid-pointpotential of Epi-Fe2+ complex equals -582 mV (vs. standard hydrogen electrode). This value ofmid-point potential explains the oxidation promotion. Biological effects/efficiency of epinephrineare influenced by its interaction with iron. Iron binding effects on biological performance ofepinephrine were examined using patch clamping in cell culture with constitutive expression ofadrenergic receptors. Epinephrine, on its own, induced an increase of outward currents, whereasEpi-Fe3+ complex did not evoke similar phenomenon. These imply that the binding of epinephrineto adrenergic receptors and their activation is inhibited by the formation of the complex of Epi withiron. Oxidative promoting activity of Fe2+ in the presence epinephrine may represent a basis forcardiovascular problems caused by chronic stress. The results obtained in this dissertation indicatethat the labile iron pool may have a new function that represents a modulation of the activity ofbiologically significant ligands/molecules.Epinephrine (Epi) is a catecholamine with important physiological roles. Interactions withother molecules and associated biological effects of Epi are controlled by its molecularconformation. Coordinate interactions of epinephrine with iron at physiological pH and their redoxactivity are crucial for understanding two distinct phenomena. First, the adverse effects that chronicstress causes to cardiovascular system. Second, the cross-linking of biopolymers and frameworkswhich are rich in catecholamines. Conformation of epinephrine in polar solvents, namely indimethyl sulfoxide (DMSO) and water, was investigated in order to shed light on effects solventsand hydrogen bonds exert on interactions of epinephrine with iron.Mechanism of epinephrine interactions with Fe2+ and Fe3+ ions was studied at differentconcentration ratios, at physiological pH (pH 7.4), and the results are presented in this dissertation.For the sake of exploration of biological effects of epinephrine, this dissertation also contains theresults of examination of effects Epi-Fe3+ complex has on cell culture with constitutive expressionof adrenergic receptors.Conformation of epinephrine in polar solvents, namely in dimethyl sulfoxide (DMSO) andwater, was investigated using 1H NMR, 1H - 1H COSY, NOESY and 1H - 15N HSQC methods.When DMSO was used as a solvent, chemical and magnetic nonequivalence of protons was spottedat NH2 and CH2 groups on epinephrine. Characteristics of hydrogen bonds in DMSO weredetermined by studying effect which temperature rise has on NMR spectra and also analyzinginfluences of solvent substitution on NMR spectra. Results have shown that epinephrine inducesstrong intramolecular bond between one of the protons of NH2 group and the OH group on the sidechain. On the other hand, the OH group on the side chain, i.e. the aliphatic OH group, presents aproton donor for intermolecular bond between epinephrine and DMSO. This phenomenon was notnoticed when water was used as a solvent. 3D modelling of epinephrine molecule structure wasbased on information about spatial arrangement of protons, which in turn was obtained usingNOESY method. Obtained 3D model shows that epinephrine in DMSO has a rigid structure thatresembles the shape of a scorpion, in which the catechol ring presents the body of the scorpion andthe side chain presents the tail of the scorpion. This structure is a consequence of formation of anadditional five–membered ring limited by inter/intra–molecular bonds. If water is used as a solvent(instead of DMSO), epinephrine takes different and non-rigid conformation which does not possessthe aforementioned intramolecular hydrogen bond. In this case, conformation of epinephrine isdetermined by hydrogen bonds with solvent molecules.Examinations conducted in the scope of this dissertation showed that epinephrine and Fe3+form stable high-spin complexes in 1:1 and 3:1 stoichiometry. Stoichiometry of these depends onconcentration ratio of epinephrine and Fe3+. Results acquired using Raman spectroscopy haveshown that 1:1 bidentate Epi–Fe3+ complex is formed by coordinative bonding of Fe3+ ions toepinephrine molecule through O atoms on the catechol ring. Effect of Fe3+ and Fe2+ ions on redoxproperties of epinephrine was studied using method of cyclic voltammetry. It was observed thatFe3+ ions do not significantly affect redox properties of epinephrine, but epinephrine with Fe2+ ionsforms strong reducing agent. Fe2+ ion presents electron donor that in the presence of epinephrinereduces O2 and causes production of H2O2. Specific hemism of epinephrine, which includesoxidation of Fe2+ ions, may present a mechanism that explains stress-induced cardiotoxicity andheart diseases. Also, these results can be used for improvement of synthesis and development ofbiopolymers.viIn stressful situations epinephrine is released and it may interact with labile iron in humanblood plasma. These interactions can have potentially important (patho)physiological effects. In thisdissertation, it is shown that at physiological pH epinephrine and Fe3+ build stable 1:1 high-spinbidentate complex. It is also shown that in presence of iron, at physiological pH, epinephrine doesnot degrade. It was observed that epinephrine and Fe2+ build colorless complex, which was stableunder anaerobic conditions. In presence of O2, epinephrine significantly catalyzed oxidation of Fe2+ions and formation of Epi-Fe3+ complex. Cyclic voltammetry results showed that the mid-pointpotential of Epi-Fe2+ complex equals -582 mV (vs. standard hydrogen electrode). This value ofmid-point potential explains the oxidation promotion. Biological effects/efficiency of epinephrineare influenced by its interaction with iron. Iron binding effects on biological performance ofepinephrine were examined using patch clamping in cell culture with constitutive expression ofadrenergic receptors. Epinephrine, on its own, induced an increase of outward currents, whereasEpi-Fe3+ complex did not evoke similar phenomenon. These imply that the binding of epinephrineto adrenergic receptors and their activation is inhibited by the formation of the complex of Epi withiron. Oxidative promoting activity of Fe2+ in the presence epinephrine may represent a basis forcardiovascular problems caused by chronic stress. The results obtained in this dissertation indicatethat the labile iron pool may have a new function that represents a modulation of the activity ofbiologically significant ligands/molecules.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Ispitivanje koordinativnih sposobnosti epinefrina prema Fe2+ i Fe3+ katjonima i redoks aktivnost nastalih kompleksa"
}
Korać Jačić, J. K.. (2020). Ispitivanje koordinativnih sposobnosti epinefrina prema Fe2+ i Fe3+ katjonima i redoks aktivnost nastalih kompleksa. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Korać Jačić JK. Ispitivanje koordinativnih sposobnosti epinefrina prema Fe2+ i Fe3+ katjonima i redoks aktivnost nastalih kompleksa. in Универзитет у Београду. 2020;..
Korać Jačić, Jelena K., "Ispitivanje koordinativnih sposobnosti epinefrina prema Fe2+ i Fe3+ katjonima i redoks aktivnost nastalih kompleksa" in Универзитет у Београду (2020).

Supplementary data for the article: Smailagić, A.; Veljović, S.; Gašić, U. M.; Dabić-Zagorac, D.; Stanković, M.; Radotić, K.; Natić, M. Phenolic Profile, Chromatic Parameters and Fluorescence of Different Woods Used in Balkan Cooperage. Industrial Crops and Products 2019, 132, 156–167. https://doi.org/10.1016/j.indcrop.2019.02.017

Smailagić, Anita; Veljović, Sonja; Gašić, Uroš M.; Dabić-Zagorac, Dragana; Stanković, Mira; Radotić, Ksenija; Natić, Maja

(Elsevier, 2019)

TY  - DATA
AU  - Smailagić, Anita
AU  - Veljović, Sonja
AU  - Gašić, Uroš M.
AU  - Dabić-Zagorac, Dragana
AU  - Stanković, Mira
AU  - Radotić, Ksenija
AU  - Natić, Maja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3921
PB  - Elsevier
T2  - Industrial Crops and Products
T1  - Supplementary data for the article: Smailagić, A.; Veljović, S.; Gašić, U. M.; Dabić-Zagorac, D.; Stanković, M.; Radotić, K.; Natić, M. Phenolic Profile, Chromatic Parameters and Fluorescence of Different Woods Used in Balkan Cooperage. Industrial Crops and Products 2019, 132, 156–167. https://doi.org/10.1016/j.indcrop.2019.02.017
ER  - 
@misc{
author = "Smailagić, Anita and Veljović, Sonja and Gašić, Uroš M. and Dabić-Zagorac, Dragana and Stanković, Mira and Radotić, Ksenija and Natić, Maja",
year = "2019",
publisher = "Elsevier",
journal = "Industrial Crops and Products",
title = "Supplementary data for the article: Smailagić, A.; Veljović, S.; Gašić, U. M.; Dabić-Zagorac, D.; Stanković, M.; Radotić, K.; Natić, M. Phenolic Profile, Chromatic Parameters and Fluorescence of Different Woods Used in Balkan Cooperage. Industrial Crops and Products 2019, 132, 156–167. https://doi.org/10.1016/j.indcrop.2019.02.017"
}
Smailagić, A., Veljović, S., Gašić, U. M., Dabić-Zagorac, D., Stanković, M., Radotić, K.,& Natić, M.. (2019). Supplementary data for the article: Smailagić, A.; Veljović, S.; Gašić, U. M.; Dabić-Zagorac, D.; Stanković, M.; Radotić, K.; Natić, M. Phenolic Profile, Chromatic Parameters and Fluorescence of Different Woods Used in Balkan Cooperage. Industrial Crops and Products 2019, 132, 156–167. https://doi.org/10.1016/j.indcrop.2019.02.017. in Industrial Crops and Products
Elsevier..
Smailagić A, Veljović S, Gašić UM, Dabić-Zagorac D, Stanković M, Radotić K, Natić M. Supplementary data for the article: Smailagić, A.; Veljović, S.; Gašić, U. M.; Dabić-Zagorac, D.; Stanković, M.; Radotić, K.; Natić, M. Phenolic Profile, Chromatic Parameters and Fluorescence of Different Woods Used in Balkan Cooperage. Industrial Crops and Products 2019, 132, 156–167. https://doi.org/10.1016/j.indcrop.2019.02.017. in Industrial Crops and Products. 2019;..
Smailagić, Anita, Veljović, Sonja, Gašić, Uroš M., Dabić-Zagorac, Dragana, Stanković, Mira, Radotić, Ksenija, Natić, Maja, "Supplementary data for the article: Smailagić, A.; Veljović, S.; Gašić, U. M.; Dabić-Zagorac, D.; Stanković, M.; Radotić, K.; Natić, M. Phenolic Profile, Chromatic Parameters and Fluorescence of Different Woods Used in Balkan Cooperage. Industrial Crops and Products 2019, 132, 156–167. https://doi.org/10.1016/j.indcrop.2019.02.017" in Industrial Crops and Products (2019).

Effects of Ag+ ion doping on UV radiation absorption and luminescence profiles of fluorapatite nanomaterials obtained by neutralization method

Milojkov, Dušan; Stanić, Vojislav; Dimović, Slavko; Mutavdžić, Dragosav; Živković-Radovanović, Vukosava; Janjić, Goran V.; Radotić, Ksenija

(Polish Academy of Sciences, 2019)

TY  - JOUR
AU  - Milojkov, Dušan
AU  - Stanić, Vojislav
AU  - Dimović, Slavko
AU  - Mutavdžić, Dragosav
AU  - Živković-Radovanović, Vukosava
AU  - Janjić, Goran V.
AU  - Radotić, Ksenija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3717
AB  - In the present study we have analyzed effects of Ag+ ions doping on energetic profiles of nanophosphors materials based on fluorapatite crystal system. The UV radiation absorption and luminescence properties of monophase fluorapatite (FAP) and Ag+ doped fluorapatite (AgFAP) nanomaterials obtained by neutralization method were investigated using the photoluminescence spectrophotometry. The excitation-emission profiles of nanomaterials were analyzed statistically by MCR-ALS method and number of fluorophores was extracted. FAP lattice absorbed light at 350 nm in the UVA part of spectrum, and with increasing concentration of Ag+ ions new absorption maximum appeared at 270 nm in the UVC part. Fluorescence of FAP nanoparticles was in violet region of visible part of the spectrum, with a red shift to the green region when Ag+ was doped in lattice. MCR-ALS analyses of fluorescence spectra confirm formation of two maxima, at 484 and 505 nm, as a consequence of Ag+ ions doping in FAP lattice at Ca1 (4f) sites. The results of quantum chemical calculations showed that an Ag+ ion is stronger bonded to the binding site 1 (-1352:6 kcal/mol) than to the binding site 2 (-1249:0 kcal/mol). Considering that AgFAP1 nanopowder absorbs photons over all part of UV radiation spectrum, this material might be used as potential radiation protective nanomaterial.
PB  - Polish Academy of Sciences
T2  - Acta Physica Polonica A
T1  - Effects of Ag+ ion doping on UV radiation absorption and luminescence profiles of fluorapatite nanomaterials obtained by neutralization method
VL  - 136
IS  - 1
SP  - 86
EP  - 91
DO  - 10.12693/APhysPolA.136.86
ER  - 
@article{
author = "Milojkov, Dušan and Stanić, Vojislav and Dimović, Slavko and Mutavdžić, Dragosav and Živković-Radovanović, Vukosava and Janjić, Goran V. and Radotić, Ksenija",
year = "2019",
abstract = "In the present study we have analyzed effects of Ag+ ions doping on energetic profiles of nanophosphors materials based on fluorapatite crystal system. The UV radiation absorption and luminescence properties of monophase fluorapatite (FAP) and Ag+ doped fluorapatite (AgFAP) nanomaterials obtained by neutralization method were investigated using the photoluminescence spectrophotometry. The excitation-emission profiles of nanomaterials were analyzed statistically by MCR-ALS method and number of fluorophores was extracted. FAP lattice absorbed light at 350 nm in the UVA part of spectrum, and with increasing concentration of Ag+ ions new absorption maximum appeared at 270 nm in the UVC part. Fluorescence of FAP nanoparticles was in violet region of visible part of the spectrum, with a red shift to the green region when Ag+ was doped in lattice. MCR-ALS analyses of fluorescence spectra confirm formation of two maxima, at 484 and 505 nm, as a consequence of Ag+ ions doping in FAP lattice at Ca1 (4f) sites. The results of quantum chemical calculations showed that an Ag+ ion is stronger bonded to the binding site 1 (-1352:6 kcal/mol) than to the binding site 2 (-1249:0 kcal/mol). Considering that AgFAP1 nanopowder absorbs photons over all part of UV radiation spectrum, this material might be used as potential radiation protective nanomaterial.",
publisher = "Polish Academy of Sciences",
journal = "Acta Physica Polonica A",
title = "Effects of Ag+ ion doping on UV radiation absorption and luminescence profiles of fluorapatite nanomaterials obtained by neutralization method",
volume = "136",
number = "1",
pages = "86-91",
doi = "10.12693/APhysPolA.136.86"
}
Milojkov, D., Stanić, V., Dimović, S., Mutavdžić, D., Živković-Radovanović, V., Janjić, G. V.,& Radotić, K.. (2019). Effects of Ag+ ion doping on UV radiation absorption and luminescence profiles of fluorapatite nanomaterials obtained by neutralization method. in Acta Physica Polonica A
Polish Academy of Sciences., 136(1), 86-91.
https://doi.org/10.12693/APhysPolA.136.86
Milojkov D, Stanić V, Dimović S, Mutavdžić D, Živković-Radovanović V, Janjić GV, Radotić K. Effects of Ag+ ion doping on UV radiation absorption and luminescence profiles of fluorapatite nanomaterials obtained by neutralization method. in Acta Physica Polonica A. 2019;136(1):86-91.
doi:10.12693/APhysPolA.136.86 .
Milojkov, Dušan, Stanić, Vojislav, Dimović, Slavko, Mutavdžić, Dragosav, Živković-Radovanović, Vukosava, Janjić, Goran V., Radotić, Ksenija, "Effects of Ag+ ion doping on UV radiation absorption and luminescence profiles of fluorapatite nanomaterials obtained by neutralization method" in Acta Physica Polonica A, 136, no. 1 (2019):86-91,
https://doi.org/10.12693/APhysPolA.136.86 . .
1
1

Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis

Stanković, M.; Bartolić, D.; Šikoparija, Branko; Spasojević, Dragica; Mutavdžić, Dragosav; Natić, Maja; Radotić, Ksenija

(2019)

TY  - JOUR
AU  - Stanković, M.
AU  - Bartolić, D.
AU  - Šikoparija, Branko
AU  - Spasojević, Dragica
AU  - Mutavdžić, Dragosav
AU  - Natić, Maja
AU  - Radotić, Ksenija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3115
AB  - It has been explored to what extent the ratio of the two main fluorophores in honey, originating from proteins and phenolic compounds, change between the honey extraction stage and packaging in the jars. Fluorescence spectroscopy combined with multivariate curve resolution–alternating least squares (MCR–ALS) was used to determine the ratio of the spectral components originating from phenol and proteins (Ph/Pr) fl , as a ratiometric indicator of variability in selected Lime tree (Tilia L.) honey samples. Spectrophotometric quantification of phenols and proteins in the honey samples was also performed and their ratio (Ph/Pr) sp was calculated. The values of the (Ph/Pr) fl ratio and honey protein content after packaging depended on the quality of homogenization before packaging in jars. Colorimetric and fluorometric results for phenols and proteins were in compliance. The examples are the values 3.34, 3.30, and 9, 3.14 for (Ph/Pr) fl and corresponding values 2.64, 2.18, and 12.75, 2.31 for (Ph/Pr) sp , in all pairs, the first value presenting the sample after extraction and the second value the sample after packaging in jars. Both methods show that in the former case there is no change in the phenol/protein ratio, and in the latter case the ratio decreased.
T2  - Journal of Applied Spectroscopy
T1  - Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis
VL  - 86
IS  - 2
SP  - 256
EP  - 263
DO  - 10.1007/s10812-019-00809-1
ER  - 
@article{
author = "Stanković, M. and Bartolić, D. and Šikoparija, Branko and Spasojević, Dragica and Mutavdžić, Dragosav and Natić, Maja and Radotić, Ksenija",
year = "2019",
abstract = "It has been explored to what extent the ratio of the two main fluorophores in honey, originating from proteins and phenolic compounds, change between the honey extraction stage and packaging in the jars. Fluorescence spectroscopy combined with multivariate curve resolution–alternating least squares (MCR–ALS) was used to determine the ratio of the spectral components originating from phenol and proteins (Ph/Pr) fl , as a ratiometric indicator of variability in selected Lime tree (Tilia L.) honey samples. Spectrophotometric quantification of phenols and proteins in the honey samples was also performed and their ratio (Ph/Pr) sp was calculated. The values of the (Ph/Pr) fl ratio and honey protein content after packaging depended on the quality of homogenization before packaging in jars. Colorimetric and fluorometric results for phenols and proteins were in compliance. The examples are the values 3.34, 3.30, and 9, 3.14 for (Ph/Pr) fl and corresponding values 2.64, 2.18, and 12.75, 2.31 for (Ph/Pr) sp , in all pairs, the first value presenting the sample after extraction and the second value the sample after packaging in jars. Both methods show that in the former case there is no change in the phenol/protein ratio, and in the latter case the ratio decreased.",
journal = "Journal of Applied Spectroscopy",
title = "Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis",
volume = "86",
number = "2",
pages = "256-263",
doi = "10.1007/s10812-019-00809-1"
}
Stanković, M., Bartolić, D., Šikoparija, B., Spasojević, D., Mutavdžić, D., Natić, M.,& Radotić, K.. (2019). Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis. in Journal of Applied Spectroscopy, 86(2), 256-263.
https://doi.org/10.1007/s10812-019-00809-1
Stanković M, Bartolić D, Šikoparija B, Spasojević D, Mutavdžić D, Natić M, Radotić K. Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis. in Journal of Applied Spectroscopy. 2019;86(2):256-263.
doi:10.1007/s10812-019-00809-1 .
Stanković, M., Bartolić, D., Šikoparija, Branko, Spasojević, Dragica, Mutavdžić, Dragosav, Natić, Maja, Radotić, Ksenija, "Variability Estimation of the Protein and Phenol Total Content in Honey Using Front Face Fluorescence Spectroscopy Coupled with MCR–ALS Analysis" in Journal of Applied Spectroscopy, 86, no. 2 (2019):256-263,
https://doi.org/10.1007/s10812-019-00809-1 . .
4
3
3

Interaction of carbohydrate coated cerium-oxide nanoparticles with wheat and pea: Stress induction potential and effect on development

Milenković, Ivana; Mitrović, Aleksandra D.; Algarra, Manuel; Lázaro-Martínez, Juan M.; Rodríguez-Castellón, Enrique; Maksimović, Vuk; Spasić, Slađana Z.; Beškoski, Vladimir; Radotić, Ksenija

(MDPI, 2019)

TY  - JOUR
AU  - Milenković, Ivana
AU  - Mitrović, Aleksandra D.
AU  - Algarra, Manuel
AU  - Lázaro-Martínez, Juan M.
AU  - Rodríguez-Castellón, Enrique
AU  - Maksimović, Vuk
AU  - Spasić, Slađana Z.
AU  - Beškoski, Vladimir
AU  - Radotić, Ksenija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3698
AB  - Reports about the influence of cerium-oxide nanoparticles (nCeO2) on plants are contradictory due to their positive and negative effects on plants. Surface modification may affect the interaction of nCeO2 with the environment, and hence its availability to plants. In this study, the uncoated and glucose-, levan-, and pullulan-coated nCeO2 were synthesized and characterized. The aim was to determine whether nontoxic carbohydrates alter the effect of nCeO2 on the seed germination, plant growth, and metabolism of wheat and pea. We applied 200 mgL-1 of nCeO2 on plants during germination (Ger treatment) or three week-growth (Gro treatment) in hydroponics. The plant response to nCeO2 was studied by measuring changes in Ce concentration, total antioxidative activity (TAA), total phenolic content (TPC), and phenolic profile. Our results generally revealed higher Ce concentration in plants after the treatment with coated nanoparticles compared to uncoated ones. Considering all obtained results, Ger treatment had a stronger impact on the later stages of plant development than Gro treatment. The Ger treatment had a stronger impact on TPC and plant elongation, whereas Gro treatment affected more TAA and phenolic profile. Among nanoparticles, levan-coated nCeO2 had the strongest and positive impact on tested plants. Wheat showed higher sensitivity to all treatments.
PB  - MDPI
T2  - Plants
T1  - Interaction of carbohydrate coated cerium-oxide nanoparticles with wheat and pea: Stress induction potential and effect on development
VL  - 8
IS  - 11
DO  - 10.3390/plants8110478
ER  - 
@article{
author = "Milenković, Ivana and Mitrović, Aleksandra D. and Algarra, Manuel and Lázaro-Martínez, Juan M. and Rodríguez-Castellón, Enrique and Maksimović, Vuk and Spasić, Slađana Z. and Beškoski, Vladimir and Radotić, Ksenija",
year = "2019",
abstract = "Reports about the influence of cerium-oxide nanoparticles (nCeO2) on plants are contradictory due to their positive and negative effects on plants. Surface modification may affect the interaction of nCeO2 with the environment, and hence its availability to plants. In this study, the uncoated and glucose-, levan-, and pullulan-coated nCeO2 were synthesized and characterized. The aim was to determine whether nontoxic carbohydrates alter the effect of nCeO2 on the seed germination, plant growth, and metabolism of wheat and pea. We applied 200 mgL-1 of nCeO2 on plants during germination (Ger treatment) or three week-growth (Gro treatment) in hydroponics. The plant response to nCeO2 was studied by measuring changes in Ce concentration, total antioxidative activity (TAA), total phenolic content (TPC), and phenolic profile. Our results generally revealed higher Ce concentration in plants after the treatment with coated nanoparticles compared to uncoated ones. Considering all obtained results, Ger treatment had a stronger impact on the later stages of plant development than Gro treatment. The Ger treatment had a stronger impact on TPC and plant elongation, whereas Gro treatment affected more TAA and phenolic profile. Among nanoparticles, levan-coated nCeO2 had the strongest and positive impact on tested plants. Wheat showed higher sensitivity to all treatments.",
publisher = "MDPI",
journal = "Plants",
title = "Interaction of carbohydrate coated cerium-oxide nanoparticles with wheat and pea: Stress induction potential and effect on development",
volume = "8",
number = "11",
doi = "10.3390/plants8110478"
}
Milenković, I., Mitrović, A. D., Algarra, M., Lázaro-Martínez, J. M., Rodríguez-Castellón, E., Maksimović, V., Spasić, S. Z., Beškoski, V.,& Radotić, K.. (2019). Interaction of carbohydrate coated cerium-oxide nanoparticles with wheat and pea: Stress induction potential and effect on development. in Plants
MDPI., 8(11).
https://doi.org/10.3390/plants8110478
Milenković I, Mitrović AD, Algarra M, Lázaro-Martínez JM, Rodríguez-Castellón E, Maksimović V, Spasić SZ, Beškoski V, Radotić K. Interaction of carbohydrate coated cerium-oxide nanoparticles with wheat and pea: Stress induction potential and effect on development. in Plants. 2019;8(11).
doi:10.3390/plants8110478 .
Milenković, Ivana, Mitrović, Aleksandra D., Algarra, Manuel, Lázaro-Martínez, Juan M., Rodríguez-Castellón, Enrique, Maksimović, Vuk, Spasić, Slađana Z., Beškoski, Vladimir, Radotić, Ksenija, "Interaction of carbohydrate coated cerium-oxide nanoparticles with wheat and pea: Stress induction potential and effect on development" in Plants, 8, no. 11 (2019),
https://doi.org/10.3390/plants8110478 . .
4
3
3

Supplementary data for the article: Milenković, I.; Mitrović, A.; Algarra, M.; Lázaro-Martínez, J. M.; Rodríguez-Castellón, E.; Maksimović, V.; Spasić, S. Z.; Beškoski, V. P.; Radotić, K. Interaction of Carbohydrate Coated Cerium-Oxide Nanoparticles with Wheat and Pea: Stress Induction Potential and Effect on Development. Plants 2019, 8 (11). https://doi.org/10.3390/plants8110478

Milenković, Ivana; Mitrović, Aleksandra D.; Algarra, Manuel; Lázaro-Martínez, Juan M.; Rodríguez-Castellón, Enrique; Maksimović, Vuk; Spasić, Slađana Z.; Beškoski, Vladimir; Radotić, Ksenija

(MDPI, 2019)

TY  - DATA
AU  - Milenković, Ivana
AU  - Mitrović, Aleksandra D.
AU  - Algarra, Manuel
AU  - Lázaro-Martínez, Juan M.
AU  - Rodríguez-Castellón, Enrique
AU  - Maksimović, Vuk
AU  - Spasić, Slađana Z.
AU  - Beškoski, Vladimir
AU  - Radotić, Ksenija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3699
PB  - MDPI
T2  - Plants
T1  - Supplementary data for the article: Milenković, I.; Mitrović, A.; Algarra, M.; Lázaro-Martínez, J. M.; Rodríguez-Castellón, E.; Maksimović, V.; Spasić, S. Z.; Beškoski, V. P.; Radotić, K. Interaction of Carbohydrate Coated Cerium-Oxide Nanoparticles with Wheat and Pea: Stress Induction Potential and Effect on Development. Plants 2019, 8 (11). https://doi.org/10.3390/plants8110478
ER  - 
@misc{
author = "Milenković, Ivana and Mitrović, Aleksandra D. and Algarra, Manuel and Lázaro-Martínez, Juan M. and Rodríguez-Castellón, Enrique and Maksimović, Vuk and Spasić, Slađana Z. and Beškoski, Vladimir and Radotić, Ksenija",
year = "2019",
publisher = "MDPI",
journal = "Plants",
title = "Supplementary data for the article: Milenković, I.; Mitrović, A.; Algarra, M.; Lázaro-Martínez, J. M.; Rodríguez-Castellón, E.; Maksimović, V.; Spasić, S. Z.; Beškoski, V. P.; Radotić, K. Interaction of Carbohydrate Coated Cerium-Oxide Nanoparticles with Wheat and Pea: Stress Induction Potential and Effect on Development. Plants 2019, 8 (11). https://doi.org/10.3390/plants8110478"
}
Milenković, I., Mitrović, A. D., Algarra, M., Lázaro-Martínez, J. M., Rodríguez-Castellón, E., Maksimović, V., Spasić, S. Z., Beškoski, V.,& Radotić, K.. (2019). Supplementary data for the article: Milenković, I.; Mitrović, A.; Algarra, M.; Lázaro-Martínez, J. M.; Rodríguez-Castellón, E.; Maksimović, V.; Spasić, S. Z.; Beškoski, V. P.; Radotić, K. Interaction of Carbohydrate Coated Cerium-Oxide Nanoparticles with Wheat and Pea: Stress Induction Potential and Effect on Development. Plants 2019, 8 (11). https://doi.org/10.3390/plants8110478. in Plants
MDPI..
Milenković I, Mitrović AD, Algarra M, Lázaro-Martínez JM, Rodríguez-Castellón E, Maksimović V, Spasić SZ, Beškoski V, Radotić K. Supplementary data for the article: Milenković, I.; Mitrović, A.; Algarra, M.; Lázaro-Martínez, J. M.; Rodríguez-Castellón, E.; Maksimović, V.; Spasić, S. Z.; Beškoski, V. P.; Radotić, K. Interaction of Carbohydrate Coated Cerium-Oxide Nanoparticles with Wheat and Pea: Stress Induction Potential and Effect on Development. Plants 2019, 8 (11). https://doi.org/10.3390/plants8110478. in Plants. 2019;..
Milenković, Ivana, Mitrović, Aleksandra D., Algarra, Manuel, Lázaro-Martínez, Juan M., Rodríguez-Castellón, Enrique, Maksimović, Vuk, Spasić, Slađana Z., Beškoski, Vladimir, Radotić, Ksenija, "Supplementary data for the article: Milenković, I.; Mitrović, A.; Algarra, M.; Lázaro-Martínez, J. M.; Rodríguez-Castellón, E.; Maksimović, V.; Spasić, S. Z.; Beškoski, V. P.; Radotić, K. Interaction of Carbohydrate Coated Cerium-Oxide Nanoparticles with Wheat and Pea: Stress Induction Potential and Effect on Development. Plants 2019, 8 (11). https://doi.org/10.3390/plants8110478" in Plants (2019).

Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation

Spasojević, Dragica; Prokopijević, Miloš; Prodanović, Olivera; Zelenović, Nevena D.; Polović, Natalija; Radotić, Ksenija; Prodanović, Radivoje

(The Polymer Society of Korea, 2019)

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Zelenović, Nevena D.
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3732
AB  - Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.
PB  - The Polymer Society of Korea
T2  - Macromolecular Research
T1  - Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation
VL  - 27
IS  - 8
SP  - 764
EP  - 771
DO  - 10.1007/s13233-019-7111-7
ER  - 
@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Zelenović, Nevena D. and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2019",
abstract = "Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.",
publisher = "The Polymer Society of Korea",
journal = "Macromolecular Research",
title = "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation",
volume = "27",
number = "8",
pages = "764-771",
doi = "10.1007/s13233-019-7111-7"
}
Spasojević, D., Prokopijević, M., Prodanović, O., Zelenović, N. D., Polović, N., Radotić, K.,& Prodanović, R.. (2019). Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research
The Polymer Society of Korea., 27(8), 764-771.
https://doi.org/10.1007/s13233-019-7111-7
Spasojević D, Prokopijević M, Prodanović O, Zelenović ND, Polović N, Radotić K, Prodanović R. Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. in Macromolecular Research. 2019;27(8):764-771.
doi:10.1007/s13233-019-7111-7 .
Spasojević, Dragica, Prokopijević, Miloš, Prodanović, Olivera, Zelenović, Nevena D., Polović, Natalija, Radotić, Ksenija, Prodanović, Radivoje, "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation" in Macromolecular Research, 27, no. 8 (2019):764-771,
https://doi.org/10.1007/s13233-019-7111-7 . .
3
2
3

Protein engineering of cellobiose dehydrogenase from Phanerochaete chrysosporium in yeast Saccharomyces cerevisiae InvSc1 for increased activity and stability

Blažić, Marija; Balaž, Ana Marija; Tadić, Vojin; Draganić, Bojana; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2019)

TY  - JOUR
AU  - Blažić, Marija
AU  - Balaž, Ana Marija
AU  - Tadić, Vojin
AU  - Draganić, Bojana
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2898
AB  - Cellobiose dehydrogenase (CDH) can be used in industry for lactobionic acid production, as a part of biosensors for disaccharides and in wound healing. In fungi it is involved in lignocellulose degradation. CDH gene from Phanerochaete chrysosporium has been cloned in pYES2 plasmid for extracellular expression and protein engineering in yeast Saccharomyces cerevisiae InvSC1 for the first time. A CDH gene library was generated using error-prone PCR and screened by spectrophotometric enzymatic assay based on 2,6-dichloroindophenol reduction detection in microtiter plates. Several mutants with increased activity and specificity towards lactose and cellobiose were found, purified and characterized in detail. Recombinant CDH enzymes showed a broad molecular weight between 120 and 150 KDa due to hyper-glycosylation and the best S137 N mutant showed 2.2 times increased k cat and 1.5 and 2 times increased specificity constant for lactose and cellobiose compared to the wild type enzyme. pH optimum of mutants was not changed while thermostability of selected mutants improved and S137 N mutant retained 30% of it's original activity after 15 min at 70 °C compared to 10% of activity that the wild type enzyme retained. Mutants M65S and S137 N showed also 1.6 and 1.5 times increased productivity of hydrogen peroxide in the presence of 30 mM lactose compared to the wild type.
PB  - Elsevier
T2  - Biochemical Engineering Journal
T1  - Protein engineering of cellobiose dehydrogenase from Phanerochaete chrysosporium in yeast Saccharomyces cerevisiae InvSc1 for increased activity and stability
VL  - 146
SP  - 179
EP  - 185
DO  - 10.1016/j.bej.2019.03.025
ER  - 
@article{
author = "Blažić, Marija and Balaž, Ana Marija and Tadić, Vojin and Draganić, Bojana and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
abstract = "Cellobiose dehydrogenase (CDH) can be used in industry for lactobionic acid production, as a part of biosensors for disaccharides and in wound healing. In fungi it is involved in lignocellulose degradation. CDH gene from Phanerochaete chrysosporium has been cloned in pYES2 plasmid for extracellular expression and protein engineering in yeast Saccharomyces cerevisiae InvSC1 for the first time. A CDH gene library was generated using error-prone PCR and screened by spectrophotometric enzymatic assay based on 2,6-dichloroindophenol reduction detection in microtiter plates. Several mutants with increased activity and specificity towards lactose and cellobiose were found, purified and characterized in detail. Recombinant CDH enzymes showed a broad molecular weight between 120 and 150 KDa due to hyper-glycosylation and the best S137 N mutant showed 2.2 times increased k cat and 1.5 and 2 times increased specificity constant for lactose and cellobiose compared to the wild type enzyme. pH optimum of mutants was not changed while thermostability of selected mutants improved and S137 N mutant retained 30% of it's original activity after 15 min at 70 °C compared to 10% of activity that the wild type enzyme retained. Mutants M65S and S137 N showed also 1.6 and 1.5 times increased productivity of hydrogen peroxide in the presence of 30 mM lactose compared to the wild type.",
publisher = "Elsevier",
journal = "Biochemical Engineering Journal",
title = "Protein engineering of cellobiose dehydrogenase from Phanerochaete chrysosporium in yeast Saccharomyces cerevisiae InvSc1 for increased activity and stability",
volume = "146",
pages = "179-185",
doi = "10.1016/j.bej.2019.03.025"
}
Blažić, M., Balaž, A. M., Tadić, V., Draganić, B., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Protein engineering of cellobiose dehydrogenase from Phanerochaete chrysosporium in yeast Saccharomyces cerevisiae InvSc1 for increased activity and stability. in Biochemical Engineering Journal
Elsevier., 146, 179-185.
https://doi.org/10.1016/j.bej.2019.03.025
Blažić M, Balaž AM, Tadić V, Draganić B, Ostafe R, Fischer R, Prodanović R. Protein engineering of cellobiose dehydrogenase from Phanerochaete chrysosporium in yeast Saccharomyces cerevisiae InvSc1 for increased activity and stability. in Biochemical Engineering Journal. 2019;146:179-185.
doi:10.1016/j.bej.2019.03.025 .
Blažić, Marija, Balaž, Ana Marija, Tadić, Vojin, Draganić, Bojana, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Protein engineering of cellobiose dehydrogenase from Phanerochaete chrysosporium in yeast Saccharomyces cerevisiae InvSc1 for increased activity and stability" in Biochemical Engineering Journal, 146 (2019):179-185,
https://doi.org/10.1016/j.bej.2019.03.025 . .
8
6
7

Supplementary data for the article: Kostić, A. Ž.; Gašić, U. M.; Pešić, M. B.; Stanojević, S. P.; Barać, M. B.; Mačukanović-Jocić, M. P.; Avramov, S. N.; Tešić, Ž. L. Phytochemical Analysis and Total Antioxidant Capacity of Rhizome, Above-Ground Vegetative Parts and Flower of Three Iris Species. Chemistry and Biodiversity 2019, 16 (3), 1–17. https://doi.org/10.1002/cbdv.201800565

Blažić, Marija; Balaž, Ana Marija; Tadić, Vojin; Draganić, Bojana; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2019)

TY  - DATA
AU  - Blažić, Marija
AU  - Balaž, Ana Marija
AU  - Tadić, Vojin
AU  - Draganić, Bojana
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2900
PB  - Elsevier
T2  - Biochemical Engineering Journal
T1  - Supplementary data for the article: Kostić, A. Ž.; Gašić, U. M.; Pešić, M. B.; Stanojević, S. P.; Barać, M. B.; Mačukanović-Jocić, M. P.; Avramov, S. N.; Tešić, Ž. L. Phytochemical Analysis and Total Antioxidant Capacity of Rhizome, Above-Ground Vegetative Parts and Flower of Three Iris Species. Chemistry and Biodiversity 2019, 16 (3), 1–17. https://doi.org/10.1002/cbdv.201800565
ER  - 
@misc{
author = "Blažić, Marija and Balaž, Ana Marija and Tadić, Vojin and Draganić, Bojana and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
publisher = "Elsevier",
journal = "Biochemical Engineering Journal",
title = "Supplementary data for the article: Kostić, A. Ž.; Gašić, U. M.; Pešić, M. B.; Stanojević, S. P.; Barać, M. B.; Mačukanović-Jocić, M. P.; Avramov, S. N.; Tešić, Ž. L. Phytochemical Analysis and Total Antioxidant Capacity of Rhizome, Above-Ground Vegetative Parts and Flower of Three Iris Species. Chemistry and Biodiversity 2019, 16 (3), 1–17. https://doi.org/10.1002/cbdv.201800565"
}
Blažić, M., Balaž, A. M., Tadić, V., Draganić, B., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Supplementary data for the article: Kostić, A. Ž.; Gašić, U. M.; Pešić, M. B.; Stanojević, S. P.; Barać, M. B.; Mačukanović-Jocić, M. P.; Avramov, S. N.; Tešić, Ž. L. Phytochemical Analysis and Total Antioxidant Capacity of Rhizome, Above-Ground Vegetative Parts and Flower of Three Iris Species. Chemistry and Biodiversity 2019, 16 (3), 1–17. https://doi.org/10.1002/cbdv.201800565. in Biochemical Engineering Journal
Elsevier..
Blažić M, Balaž AM, Tadić V, Draganić B, Ostafe R, Fischer R, Prodanović R. Supplementary data for the article: Kostić, A. Ž.; Gašić, U. M.; Pešić, M. B.; Stanojević, S. P.; Barać, M. B.; Mačukanović-Jocić, M. P.; Avramov, S. N.; Tešić, Ž. L. Phytochemical Analysis and Total Antioxidant Capacity of Rhizome, Above-Ground Vegetative Parts and Flower of Three Iris Species. Chemistry and Biodiversity 2019, 16 (3), 1–17. https://doi.org/10.1002/cbdv.201800565. in Biochemical Engineering Journal. 2019;..
Blažić, Marija, Balaž, Ana Marija, Tadić, Vojin, Draganić, Bojana, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Supplementary data for the article: Kostić, A. Ž.; Gašić, U. M.; Pešić, M. B.; Stanojević, S. P.; Barać, M. B.; Mačukanović-Jocić, M. P.; Avramov, S. N.; Tešić, Ž. L. Phytochemical Analysis and Total Antioxidant Capacity of Rhizome, Above-Ground Vegetative Parts and Flower of Three Iris Species. Chemistry and Biodiversity 2019, 16 (3), 1–17. https://doi.org/10.1002/cbdv.201800565" in Biochemical Engineering Journal (2019).

Directed evolution of cellobiose dehydrogenase on the surface of yeast cells using resazurin-based fluorescent assay

Blažić, Marija; Balaž, Ana Marija; Prodanović, Olivera; Popović, Nikolina; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(Applied sciences, 2019)

TY  - JOUR
AU  - Blažić, Marija
AU  - Balaž, Ana Marija
AU  - Prodanović, Olivera
AU  - Popović, Nikolina
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2909
AB  - Cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium can be used in lactobionic acid production, biosensor for lactose, biofuel cells, lignocellulose degradation, and wound-healing applications. To make it a better biocatalyst, CDH with higher activity in an immobilized form is desirable. For this purpose, CDH was expressed for the first time on the surface of S. cerevisiae EBY100 cells in an active form as a triple mutant tmCDH (D20N, A64T, V592M) and evolved further for higher activity using resazurin-based fluorescent assay. In order to decrease blank reaction of resazurin with yeast cells and to have linear correlation between enzyme activity on the cell surface and fluorescence signal, the assay was optimized with respect to resazurin concentration (0.1 mM), substrate concentration (10mMlactose and 0.08mMcellobiose), and pH (6.0). Using optimized assay an error prone PCR gene library of tmCDH was screened. Two mutants with 5 (H5) and 7 mutations (H9) were found having two times higher activity than the parent tmCDH enzyme that already had improved activity compared to wild type CDH whose activity could not be detected on the surface of yeast cells.
PB  - Applied sciences
T2  - Applied Sciences (Switzerland)
T1  - Directed evolution of cellobiose dehydrogenase on the surface of yeast cells using resazurin-based fluorescent assay
VL  - 9
IS  - 7
SP  - 1
EP  - 15
DO  - 10.3390/app9071413
ER  - 
@article{
author = "Blažić, Marija and Balaž, Ana Marija and Prodanović, Olivera and Popović, Nikolina and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
abstract = "Cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium can be used in lactobionic acid production, biosensor for lactose, biofuel cells, lignocellulose degradation, and wound-healing applications. To make it a better biocatalyst, CDH with higher activity in an immobilized form is desirable. For this purpose, CDH was expressed for the first time on the surface of S. cerevisiae EBY100 cells in an active form as a triple mutant tmCDH (D20N, A64T, V592M) and evolved further for higher activity using resazurin-based fluorescent assay. In order to decrease blank reaction of resazurin with yeast cells and to have linear correlation between enzyme activity on the cell surface and fluorescence signal, the assay was optimized with respect to resazurin concentration (0.1 mM), substrate concentration (10mMlactose and 0.08mMcellobiose), and pH (6.0). Using optimized assay an error prone PCR gene library of tmCDH was screened. Two mutants with 5 (H5) and 7 mutations (H9) were found having two times higher activity than the parent tmCDH enzyme that already had improved activity compared to wild type CDH whose activity could not be detected on the surface of yeast cells.",
publisher = "Applied sciences",
journal = "Applied Sciences (Switzerland)",
title = "Directed evolution of cellobiose dehydrogenase on the surface of yeast cells using resazurin-based fluorescent assay",
volume = "9",
number = "7",
pages = "1-15",
doi = "10.3390/app9071413"
}
Blažić, M., Balaž, A. M., Prodanović, O., Popović, N., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Directed evolution of cellobiose dehydrogenase on the surface of yeast cells using resazurin-based fluorescent assay. in Applied Sciences (Switzerland)
Applied sciences., 9(7), 1-15.
https://doi.org/10.3390/app9071413
Blažić M, Balaž AM, Prodanović O, Popović N, Ostafe R, Fischer R, Prodanović R. Directed evolution of cellobiose dehydrogenase on the surface of yeast cells using resazurin-based fluorescent assay. in Applied Sciences (Switzerland). 2019;9(7):1-15.
doi:10.3390/app9071413 .
Blažić, Marija, Balaž, Ana Marija, Prodanović, Olivera, Popović, Nikolina, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Directed evolution of cellobiose dehydrogenase on the surface of yeast cells using resazurin-based fluorescent assay" in Applied Sciences (Switzerland), 9, no. 7 (2019):1-15,
https://doi.org/10.3390/app9071413 . .
6
6
6

Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413

Blažić, Marija; Balaž, Ana Marija; Prodanović, Olivera; Popović, Nikolina; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(Applied sciences, 2019)

TY  - DATA
AU  - Blažić, Marija
AU  - Balaž, Ana Marija
AU  - Prodanović, Olivera
AU  - Popović, Nikolina
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2912
PB  - Applied sciences
T2  - Applied Sciences (Switzerland)
T1  - Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413
ER  - 
@misc{
author = "Blažić, Marija and Balaž, Ana Marija and Prodanović, Olivera and Popović, Nikolina and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
publisher = "Applied sciences",
journal = "Applied Sciences (Switzerland)",
title = "Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413"
}
Blažić, M., Balaž, A. M., Prodanović, O., Popović, N., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413. in Applied Sciences (Switzerland)
Applied sciences..
Blažić M, Balaž AM, Prodanović O, Popović N, Ostafe R, Fischer R, Prodanović R. Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413. in Applied Sciences (Switzerland). 2019;..
Blažić, Marija, Balaž, Ana Marija, Prodanović, Olivera, Popović, Nikolina, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Supplementary data for the article: Blažić, M.; Balaž, A. M.; Prodanović, O.; Popović, N.; Ostafe, R.; Fischer, R.; Prodanović, R. Directed Evolution of Cellobiose Dehydrogenase on the Surface of Yeast Cells Using Resazurin-Based Fluorescent Assay. Applied Sciences (Switzerland) 2019, 9 (7). https://doi.org/10.3390/app9071413" in Applied Sciences (Switzerland) (2019).

Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage

Smailagić, Anita; Veljović, Sonja; Gašić, Uroš M.; Dabić-Zagorac, Dragana; Stanković, Mira; Radotić, Ksenija; Natić, Maja

(Elsevier, 2019)

TY  - JOUR
AU  - Smailagić, Anita
AU  - Veljović, Sonja
AU  - Gašić, Uroš M.
AU  - Dabić-Zagorac, Dragana
AU  - Stanković, Mira
AU  - Radotić, Ksenija
AU  - Natić, Maja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2832
AB  - The aim of this research was to study phenolic compounds of diverse botanical species of wood commonly used in cooperage in Balkan countries. Several botanical species have been considered including mulberry (Morus alba L.), myrobalan plum (Prunus cerasifera Ehrh.), black locust (Robinia pseudoacacia L.), wild cherry (Prunus avium (L.) L.), and oak (Q. petraea (Matt.) Liebl., Q. robur L., and Q. cerris L.). A total of 37 compounds were quantified, demonstrating the presence of phenolic acids, flavonols, flavones, flavanones, flavanonol taxifolin, stilbenoids, and coumarins. Taxifolin was the most abundant in wild cherry (8455.70 mg kg−1), while ellagic acid predominated in oak wood (8872.05–10099.32 mg kg−1 in sessile oaks, and up to 15,958.80 mg kg−1 in pedunculate oak from Slavonia). The highest content of protocatechuic acid (533.39 mg kg−1) was found in myrobalan plum. Also, isoflavones were characteristic of wild cherry, while mulberry was abundant in stilbenoids. Total phenolic content, as well as antioxidant, chromatic, and fluorescence properties were studied. The spectral shapes and maxima of fluorescence emission spectra of bare wood samples were compared with those of the corresponding wood extracts. The Principal Component Analysis (PCA) was applied in order to find patterns in emission spectra for differentiation among wood samples.
PB  - Elsevier
T2  - Industrial Crops and Products
T1  - Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage
VL  - 132
SP  - 156
EP  - 167
DO  - 10.1016/j.indcrop.2019.02.017
ER  - 
@article{
author = "Smailagić, Anita and Veljović, Sonja and Gašić, Uroš M. and Dabić-Zagorac, Dragana and Stanković, Mira and Radotić, Ksenija and Natić, Maja",
year = "2019",
abstract = "The aim of this research was to study phenolic compounds of diverse botanical species of wood commonly used in cooperage in Balkan countries. Several botanical species have been considered including mulberry (Morus alba L.), myrobalan plum (Prunus cerasifera Ehrh.), black locust (Robinia pseudoacacia L.), wild cherry (Prunus avium (L.) L.), and oak (Q. petraea (Matt.) Liebl., Q. robur L., and Q. cerris L.). A total of 37 compounds were quantified, demonstrating the presence of phenolic acids, flavonols, flavones, flavanones, flavanonol taxifolin, stilbenoids, and coumarins. Taxifolin was the most abundant in wild cherry (8455.70 mg kg−1), while ellagic acid predominated in oak wood (8872.05–10099.32 mg kg−1 in sessile oaks, and up to 15,958.80 mg kg−1 in pedunculate oak from Slavonia). The highest content of protocatechuic acid (533.39 mg kg−1) was found in myrobalan plum. Also, isoflavones were characteristic of wild cherry, while mulberry was abundant in stilbenoids. Total phenolic content, as well as antioxidant, chromatic, and fluorescence properties were studied. The spectral shapes and maxima of fluorescence emission spectra of bare wood samples were compared with those of the corresponding wood extracts. The Principal Component Analysis (PCA) was applied in order to find patterns in emission spectra for differentiation among wood samples.",
publisher = "Elsevier",
journal = "Industrial Crops and Products",
title = "Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage",
volume = "132",
pages = "156-167",
doi = "10.1016/j.indcrop.2019.02.017"
}
Smailagić, A., Veljović, S., Gašić, U. M., Dabić-Zagorac, D., Stanković, M., Radotić, K.,& Natić, M.. (2019). Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage. in Industrial Crops and Products
Elsevier., 132, 156-167.
https://doi.org/10.1016/j.indcrop.2019.02.017
Smailagić A, Veljović S, Gašić UM, Dabić-Zagorac D, Stanković M, Radotić K, Natić M. Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage. in Industrial Crops and Products. 2019;132:156-167.
doi:10.1016/j.indcrop.2019.02.017 .
Smailagić, Anita, Veljović, Sonja, Gašić, Uroš M., Dabić-Zagorac, Dragana, Stanković, Mira, Radotić, Ksenija, Natić, Maja, "Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage" in Industrial Crops and Products, 132 (2019):156-167,
https://doi.org/10.1016/j.indcrop.2019.02.017 . .
10
7
8

Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage

Smailagić, Anita; Veljović, Sonja; Gašić, Uroš M.; Dabić-Zagorac, Dragana; Stanković, Mira; Radotić, Ksenija; Natić, Maja

(Elsevier, 2019)

TY  - JOUR
AU  - Smailagić, Anita
AU  - Veljović, Sonja
AU  - Gašić, Uroš M.
AU  - Dabić-Zagorac, Dragana
AU  - Stanković, Mira
AU  - Radotić, Ksenija
AU  - Natić, Maja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2835
AB  - The aim of this research was to study phenolic compounds of diverse botanical species of wood commonly used in cooperage in Balkan countries. Several botanical species have been considered including mulberry (Morus alba L.), myrobalan plum (Prunus cerasifera Ehrh.), black locust (Robinia pseudoacacia L.), wild cherry (Prunus avium (L.) L.), and oak (Q. petraea (Matt.) Liebl., Q. robur L., and Q. cerris L.). A total of 37 compounds were quantified, demonstrating the presence of phenolic acids, flavonols, flavones, flavanones, flavanonol taxifolin, stilbenoids, and coumarins. Taxifolin was the most abundant in wild cherry (8455.70 mg kg−1), while ellagic acid predominated in oak wood (8872.05–10099.32 mg kg−1 in sessile oaks, and up to 15,958.80 mg kg−1 in pedunculate oak from Slavonia). The highest content of protocatechuic acid (533.39 mg kg−1) was found in myrobalan plum. Also, isoflavones were characteristic of wild cherry, while mulberry was abundant in stilbenoids. Total phenolic content, as well as antioxidant, chromatic, and fluorescence properties were studied. The spectral shapes and maxima of fluorescence emission spectra of bare wood samples were compared with those of the corresponding wood extracts. The Principal Component Analysis (PCA) was applied in order to find patterns in emission spectra for differentiation among wood samples.
PB  - Elsevier
T2  - Industrial Crops and Products
T1  - Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage
VL  - 132
SP  - 156
EP  - 167
DO  - 10.1016/j.indcrop.2019.02.017
ER  - 
@article{
author = "Smailagić, Anita and Veljović, Sonja and Gašić, Uroš M. and Dabić-Zagorac, Dragana and Stanković, Mira and Radotić, Ksenija and Natić, Maja",
year = "2019",
abstract = "The aim of this research was to study phenolic compounds of diverse botanical species of wood commonly used in cooperage in Balkan countries. Several botanical species have been considered including mulberry (Morus alba L.), myrobalan plum (Prunus cerasifera Ehrh.), black locust (Robinia pseudoacacia L.), wild cherry (Prunus avium (L.) L.), and oak (Q. petraea (Matt.) Liebl., Q. robur L., and Q. cerris L.). A total of 37 compounds were quantified, demonstrating the presence of phenolic acids, flavonols, flavones, flavanones, flavanonol taxifolin, stilbenoids, and coumarins. Taxifolin was the most abundant in wild cherry (8455.70 mg kg−1), while ellagic acid predominated in oak wood (8872.05–10099.32 mg kg−1 in sessile oaks, and up to 15,958.80 mg kg−1 in pedunculate oak from Slavonia). The highest content of protocatechuic acid (533.39 mg kg−1) was found in myrobalan plum. Also, isoflavones were characteristic of wild cherry, while mulberry was abundant in stilbenoids. Total phenolic content, as well as antioxidant, chromatic, and fluorescence properties were studied. The spectral shapes and maxima of fluorescence emission spectra of bare wood samples were compared with those of the corresponding wood extracts. The Principal Component Analysis (PCA) was applied in order to find patterns in emission spectra for differentiation among wood samples.",
publisher = "Elsevier",
journal = "Industrial Crops and Products",
title = "Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage",
volume = "132",
pages = "156-167",
doi = "10.1016/j.indcrop.2019.02.017"
}
Smailagić, A., Veljović, S., Gašić, U. M., Dabić-Zagorac, D., Stanković, M., Radotić, K.,& Natić, M.. (2019). Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage. in Industrial Crops and Products
Elsevier., 132, 156-167.
https://doi.org/10.1016/j.indcrop.2019.02.017
Smailagić A, Veljović S, Gašić UM, Dabić-Zagorac D, Stanković M, Radotić K, Natić M. Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage. in Industrial Crops and Products. 2019;132:156-167.
doi:10.1016/j.indcrop.2019.02.017 .
Smailagić, Anita, Veljović, Sonja, Gašić, Uroš M., Dabić-Zagorac, Dragana, Stanković, Mira, Radotić, Ksenija, Natić, Maja, "Phenolic profile, chromatic parameters and fluorescence of different woods used in Balkan cooperage" in Industrial Crops and Products, 132 (2019):156-167,
https://doi.org/10.1016/j.indcrop.2019.02.017 . .
10
7
8

Influence of methionine residue position on oxidative stability of glucose oxidase from Aspergillus niger

Kovačević, Gordana; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2019)

TY  - JOUR
AU  - Kovačević, Gordana
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
AB  - Glucose oxidase (GOx) is a promising candidate for construction of implantable miniature biofuel cells and biosensors for continuous glucose monitoring. The main drawback that limits current application of GOx in these devices is its low stability, especially sensitivity to reactive oxygen species. In order to address this problem, we performed saturation mutagenesis at all 11 methionine residues as their interaction with reactive oxygen species inactivates enzymes. For successful screening of these libraries a method based on yeast surface display (YSD) systems was developed. Mutations at methionine positions close to the GOx active site contributed the most to the oxidative stability, and combinations of the four best single mutations were tested. Combined mutants did not show higher stability or activity compared to the parental single mutants. To confirm oxidative stability of YSD expressed GOx mutants they were re-cloned in Pichia pastoris, purified and immobilized on macroporous copolymer. The additional kinetic analysis of immobilized GOx mutants confirmed that the best mutant with only one mutation close to the active site (M561S) has 2.5 times increased half-life in the presence of hydrogen peroxide compared to the wild-type variant.
PB  - Elsevier
T2  - Biochemical Engineering Journal
T1  - Influence of methionine residue position on oxidative stability of glucose oxidase from Aspergillus niger
VL  - 146
SP  - 143
EP  - 149
DO  - 10.1016/j.bej.2019.03.016
ER  - 
@article{
author = "Kovačević, Gordana and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
abstract = "Glucose oxidase (GOx) is a promising candidate for construction of implantable miniature biofuel cells and biosensors for continuous glucose monitoring. The main drawback that limits current application of GOx in these devices is its low stability, especially sensitivity to reactive oxygen species. In order to address this problem, we performed saturation mutagenesis at all 11 methionine residues as their interaction with reactive oxygen species inactivates enzymes. For successful screening of these libraries a method based on yeast surface display (YSD) systems was developed. Mutations at methionine positions close to the GOx active site contributed the most to the oxidative stability, and combinations of the four best single mutations were tested. Combined mutants did not show higher stability or activity compared to the parental single mutants. To confirm oxidative stability of YSD expressed GOx mutants they were re-cloned in Pichia pastoris, purified and immobilized on macroporous copolymer. The additional kinetic analysis of immobilized GOx mutants confirmed that the best mutant with only one mutation close to the active site (M561S) has 2.5 times increased half-life in the presence of hydrogen peroxide compared to the wild-type variant.",
publisher = "Elsevier",
journal = "Biochemical Engineering Journal",
title = "Influence of methionine residue position on oxidative stability of glucose oxidase from Aspergillus niger",
volume = "146",
pages = "143-149",
doi = "10.1016/j.bej.2019.03.016"
}
Kovačević, G., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Influence of methionine residue position on oxidative stability of glucose oxidase from Aspergillus niger. in Biochemical Engineering Journal
Elsevier., 146, 143-149.
https://doi.org/10.1016/j.bej.2019.03.016
Kovačević G, Ostafe R, Fischer R, Prodanović R. Influence of methionine residue position on oxidative stability of glucose oxidase from Aspergillus niger. in Biochemical Engineering Journal. 2019;146:143-149.
doi:10.1016/j.bej.2019.03.016 .
Kovačević, Gordana, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Influence of methionine residue position on oxidative stability of glucose oxidase from Aspergillus niger" in Biochemical Engineering Journal, 146 (2019):143-149,
https://doi.org/10.1016/j.bej.2019.03.016 . .
9
7
8

Supplementary data for the article: Kovačević, G.; Ostafe, R.; Fischer, R.; Prodanović, R. Influence of Methionine Residue Position on Oxidative Stability of Glucose Oxidase from Aspergillus Niger. Biochemical Engineering Journal 2019, 146, 143–149. https://doi.org/10.1016/j.bej.2019.03.016

Kovačević, Gordana; Ostafe, Raluca; Fischer, Rainer; Prodanović, Radivoje

(Elsevier, 2019)

TY  - DATA
AU  - Kovačević, Gordana
AU  - Ostafe, Raluca
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2882
PB  - Elsevier
T2  - Biochemical Engineering Journal
T1  - Supplementary data for the article: Kovačević, G.; Ostafe, R.; Fischer, R.; Prodanović, R. Influence of Methionine Residue Position on Oxidative Stability of Glucose Oxidase from Aspergillus Niger. Biochemical Engineering Journal 2019, 146, 143–149. https://doi.org/10.1016/j.bej.2019.03.016
ER  - 
@misc{
author = "Kovačević, Gordana and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
publisher = "Elsevier",
journal = "Biochemical Engineering Journal",
title = "Supplementary data for the article: Kovačević, G.; Ostafe, R.; Fischer, R.; Prodanović, R. Influence of Methionine Residue Position on Oxidative Stability of Glucose Oxidase from Aspergillus Niger. Biochemical Engineering Journal 2019, 146, 143–149. https://doi.org/10.1016/j.bej.2019.03.016"
}
Kovačević, G., Ostafe, R., Fischer, R.,& Prodanović, R.. (2019). Supplementary data for the article: Kovačević, G.; Ostafe, R.; Fischer, R.; Prodanović, R. Influence of Methionine Residue Position on Oxidative Stability of Glucose Oxidase from Aspergillus Niger. Biochemical Engineering Journal 2019, 146, 143–149. https://doi.org/10.1016/j.bej.2019.03.016. in Biochemical Engineering Journal
Elsevier..
Kovačević G, Ostafe R, Fischer R, Prodanović R. Supplementary data for the article: Kovačević, G.; Ostafe, R.; Fischer, R.; Prodanović, R. Influence of Methionine Residue Position on Oxidative Stability of Glucose Oxidase from Aspergillus Niger. Biochemical Engineering Journal 2019, 146, 143–149. https://doi.org/10.1016/j.bej.2019.03.016. in Biochemical Engineering Journal. 2019;..
Kovačević, Gordana, Ostafe, Raluca, Fischer, Rainer, Prodanović, Radivoje, "Supplementary data for the article: Kovačević, G.; Ostafe, R.; Fischer, R.; Prodanović, R. Influence of Methionine Residue Position on Oxidative Stability of Glucose Oxidase from Aspergillus Niger. Biochemical Engineering Journal 2019, 146, 143–149. https://doi.org/10.1016/j.bej.2019.03.016" in Biochemical Engineering Journal (2019).