Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness

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Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness (en)
Развој нових инкапсулационих и ензимских технологија за производњу биокатализатора и биолошки активних компонената хране у циљу повећања њене конкурентности, квалитета и безбедности (sr)
Razvoj novih inkapsulacionih i enzimskih tehnologija za proizvodnju biokatalizatora i biološki aktivnih komponenata hrane u cilju povećanja njene konkurentnosti, kvaliteta i bezbednosti (sr_RS)
Authors

Publications

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  - BOOK
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  - 
@book{
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4103",
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.
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. 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" (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

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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4101",
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.
Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.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. Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng.. 2021;15(2):19
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" 15, no. 2 (2021):19,
https://doi.org/10.1007/s11783-020-1311-4 .
2
1

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  - BOOK
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  - 
@book{
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3836",
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.
Enzyme and Microbial TechnologyElsevier..
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. 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" (2020)

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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3834",
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.
Enzyme and Microbial TechnologyElsevier., 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. Enzyme and Microbial Technology. 2020;136:e109509
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" 136 (2020):e109509,
https://doi.org/10.1016/j.enzmictec.2020.109509 .
8
4
5

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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3835",
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.
Enzyme and Microbial TechnologyElsevier., 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. Enzyme and Microbial Technology. 2020;136:e109509
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" 136 (2020):e109509,
https://doi.org/10.1016/j.enzmictec.2020.109509 .
8
4
5

Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system

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

(Elsevier, 2020)

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ece, Selin
AU  - Ostafe, Raluca
AU  - Vogel, Simon
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3888
AB  - Pleurotus eryngii wild-type versatile peroxidase (wtVP) oxidizes structurally diverse substrates in an H2O2-dependent manner, but its ability to oxidize many pollutants is limited by suicidal enzyme inactivation in the presence of excess H2O2. To address this drawback, we generated random mutagenesis libraries containing 3 × 106 mutated VP genes and screened for enzymes with higher oxidative stability expressed on the surface of yeast cells. This was achieved by flow cytometry using the substrate fluorescein tyramide. After two rounds of sorting, the percentage of cells expressing variants with improved oxidative stability had increased from 1 % to 56 %. The most stable variants featured 3–5 amino acid substitutions and retained up to 70 % of their initial activity after incubation for 1 h in 30 mM H2O2 (conditions that completely inactivate wtVP). Selected variants were extracted from yeast cell walls and purified for kinetic characterization. We also prepared yeast cell walls with wtVP and the three most stable VP variants for multiple cycles of azo dye (Reactive black 5) degradation. After 10 cycles of 12 h, two of the variants retained more than 97 % of their initial activity, whereas the activity of wtVP declined by ∼30 %. These results confirm that our high-throughput screening system can improve the oxidative stability of versatile peroxidase, providing a source of novel enzymes for remediation applications.
PB  - Elsevier
T2  - Biochemical Engineering Journal
T1  - Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system
VL  - 157
DO  - 10.1016/j.bej.2020.107555
ER  - 
@article{
author = "Ilić Đurđić, Karla and Ece, Selin and Ostafe, Raluca and Vogel, Simon and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3888",
abstract = "Pleurotus eryngii wild-type versatile peroxidase (wtVP) oxidizes structurally diverse substrates in an H2O2-dependent manner, but its ability to oxidize many pollutants is limited by suicidal enzyme inactivation in the presence of excess H2O2. To address this drawback, we generated random mutagenesis libraries containing 3 × 106 mutated VP genes and screened for enzymes with higher oxidative stability expressed on the surface of yeast cells. This was achieved by flow cytometry using the substrate fluorescein tyramide. After two rounds of sorting, the percentage of cells expressing variants with improved oxidative stability had increased from 1 % to 56 %. The most stable variants featured 3–5 amino acid substitutions and retained up to 70 % of their initial activity after incubation for 1 h in 30 mM H2O2 (conditions that completely inactivate wtVP). Selected variants were extracted from yeast cell walls and purified for kinetic characterization. We also prepared yeast cell walls with wtVP and the three most stable VP variants for multiple cycles of azo dye (Reactive black 5) degradation. After 10 cycles of 12 h, two of the variants retained more than 97 % of their initial activity, whereas the activity of wtVP declined by ∼30 %. These results confirm that our high-throughput screening system can improve the oxidative stability of versatile peroxidase, providing a source of novel enzymes for remediation applications.",
publisher = "Elsevier",
journal = "Biochemical Engineering Journal",
title = "Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system",
volume = "157",
doi = "10.1016/j.bej.2020.107555"
}
Ilić Đurđić, K., Ece, S., Ostafe, R., Vogel, S., Schillberg, S., Fischer, R.,& Prodanović, R. (2020). Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system.
Biochemical Engineering JournalElsevier., 157.
https://doi.org/10.1016/j.bej.2020.107555
Ilić Đurđić K, Ece S, Ostafe R, Vogel S, Schillberg S, Fischer R, Prodanović R. Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system. Biochemical Engineering Journal. 2020;157
Ilić Đurđić Karla, Ece Selin, Ostafe Raluca, Vogel Simon, Schillberg Stefan, Fischer Rainer, Prodanović Radivoje, "Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system" 157 (2020),
https://doi.org/10.1016/j.bej.2020.107555 .
1
1

Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system

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

(Elsevier, 2020)

TY  - JOUR
AU  - Ilić Đurđić, Karla
AU  - Ece, Selin
AU  - Ostafe, Raluca
AU  - Vogel, Simon
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3898
AB  - Pleurotus eryngii wild-type versatile peroxidase (wtVP) oxidizes structurally diverse substrates in an H2O2-dependent manner, but its ability to oxidize many pollutants is limited by suicidal enzyme inactivation in the presence of excess H2O2. To address this drawback, we generated random mutagenesis libraries containing 3 × 106 mutated VP genes and screened for enzymes with higher oxidative stability expressed on the surface of yeast cells. This was achieved by flow cytometry using the substrate fluorescein tyramide. After two rounds of sorting, the percentage of cells expressing variants with improved oxidative stability had increased from 1 % to 56 %. The most stable variants featured 3–5 amino acid substitutions and retained up to 70 % of their initial activity after incubation for 1 h in 30 mM H2O2 (conditions that completely inactivate wtVP). Selected variants were extracted from yeast cell walls and purified for kinetic characterization. We also prepared yeast cell walls with wtVP and the three most stable VP variants for multiple cycles of azo dye (Reactive black 5) degradation. After 10 cycles of 12 h, two of the variants retained more than 97 % of their initial activity, whereas the activity of wtVP declined by ∼30 %. These results confirm that our high-throughput screening system can improve the oxidative stability of versatile peroxidase, providing a source of novel enzymes for remediation applications.
PB  - Elsevier
T2  - Biochemical Engineering Journal
T1  - Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system
VL  - 157
DO  - 10.1016/j.bej.2020.107555
ER  - 
@article{
author = "Ilić Đurđić, Karla and Ece, Selin and Ostafe, Raluca and Vogel, Simon and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3898",
abstract = "Pleurotus eryngii wild-type versatile peroxidase (wtVP) oxidizes structurally diverse substrates in an H2O2-dependent manner, but its ability to oxidize many pollutants is limited by suicidal enzyme inactivation in the presence of excess H2O2. To address this drawback, we generated random mutagenesis libraries containing 3 × 106 mutated VP genes and screened for enzymes with higher oxidative stability expressed on the surface of yeast cells. This was achieved by flow cytometry using the substrate fluorescein tyramide. After two rounds of sorting, the percentage of cells expressing variants with improved oxidative stability had increased from 1 % to 56 %. The most stable variants featured 3–5 amino acid substitutions and retained up to 70 % of their initial activity after incubation for 1 h in 30 mM H2O2 (conditions that completely inactivate wtVP). Selected variants were extracted from yeast cell walls and purified for kinetic characterization. We also prepared yeast cell walls with wtVP and the three most stable VP variants for multiple cycles of azo dye (Reactive black 5) degradation. After 10 cycles of 12 h, two of the variants retained more than 97 % of their initial activity, whereas the activity of wtVP declined by ∼30 %. These results confirm that our high-throughput screening system can improve the oxidative stability of versatile peroxidase, providing a source of novel enzymes for remediation applications.",
publisher = "Elsevier",
journal = "Biochemical Engineering Journal",
title = "Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system",
volume = "157",
doi = "10.1016/j.bej.2020.107555"
}
Ilić Đurđić, K., Ece, S., Ostafe, R., Vogel, S., Schillberg, S., Fischer, R.,& Prodanović, R. (2020). Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system.
Biochemical Engineering JournalElsevier., 157.
https://doi.org/10.1016/j.bej.2020.107555
Ilić Đurđić K, Ece S, Ostafe R, Vogel S, Schillberg S, Fischer R, Prodanović R. Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system. Biochemical Engineering Journal. 2020;157
Ilić Đurđić Karla, Ece Selin, Ostafe Raluca, Vogel Simon, Schillberg Stefan, Fischer Rainer, Prodanović Radivoje, "Improvement in oxidative stability of versatile peroxidase by flow cytometry-based high-throughput screening system" 157 (2020),
https://doi.org/10.1016/j.bej.2020.107555 .
1
1

Supplementary data for the article: Ilić Đurđić, K.; Ece, S.; Ostafe, R.; Vogel, S.; Schillberg, S.; Fischer, R.; Prodanović, R. Improvement in Oxidative Stability of Versatile Peroxidase by Flow Cytometry-Based High-Throughput Screening System. Biochemical Engineering Journal 2020, 157. https://doi.org/10.1016/j.bej.2020.107555

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

(Elsevier, 2020)

TY  - BOOK
AU  - Ilić Đurđić, Karla
AU  - Ece, Selin
AU  - Ostafe, Raluca
AU  - Vogel, Simon
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3899
PB  - Elsevier
T2  - Biochemical Engineering Journal
T1  - Supplementary data for the article: Ilić Đurđić, K.; Ece, S.; Ostafe, R.; Vogel, S.; Schillberg, S.; Fischer, R.; Prodanović, R. Improvement in Oxidative Stability of Versatile Peroxidase by Flow Cytometry-Based High-Throughput Screening System. Biochemical Engineering Journal 2020, 157. https://doi.org/10.1016/j.bej.2020.107555
ER  - 
@book{
author = "Ilić Đurđić, Karla and Ece, Selin and Ostafe, Raluca and Vogel, Simon and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3899",
publisher = "Elsevier",
journal = "Biochemical Engineering Journal",
title = "Supplementary data for the article: Ilić Đurđić, K.; Ece, S.; Ostafe, R.; Vogel, S.; Schillberg, S.; Fischer, R.; Prodanović, R. Improvement in Oxidative Stability of Versatile Peroxidase by Flow Cytometry-Based High-Throughput Screening System. Biochemical Engineering Journal 2020, 157. https://doi.org/10.1016/j.bej.2020.107555"
}
Ilić Đurđić, K., Ece, S., Ostafe, R., Vogel, S., Schillberg, S., Fischer, R.,& Prodanović, R. (2020). Supplementary data for the article: Ilić Đurđić, K.; Ece, S.; Ostafe, R.; Vogel, S.; Schillberg, S.; Fischer, R.; Prodanović, R. Improvement in Oxidative Stability of Versatile Peroxidase by Flow Cytometry-Based High-Throughput Screening System. Biochemical Engineering Journal 2020, 157. https://doi.org/10.1016/j.bej.2020.107555.
Biochemical Engineering JournalElsevier..
Ilić Đurđić K, Ece S, Ostafe R, Vogel S, Schillberg S, Fischer R, Prodanović R. Supplementary data for the article: Ilić Đurđić, K.; Ece, S.; Ostafe, R.; Vogel, S.; Schillberg, S.; Fischer, R.; Prodanović, R. Improvement in Oxidative Stability of Versatile Peroxidase by Flow Cytometry-Based High-Throughput Screening System. Biochemical Engineering Journal 2020, 157. https://doi.org/10.1016/j.bej.2020.107555. Biochemical Engineering Journal. 2020;
Ilić Đurđić Karla, Ece Selin, Ostafe Raluca, Vogel Simon, Schillberg Stefan, Fischer Rainer, Prodanović Radivoje, "Supplementary data for the article: Ilić Đurđić, K.; Ece, S.; Ostafe, R.; Vogel, S.; Schillberg, S.; Fischer, R.; Prodanović, R. Improvement in Oxidative Stability of Versatile Peroxidase by Flow Cytometry-Based High-Throughput Screening System. Biochemical Engineering Journal 2020, 157. https://doi.org/10.1016/j.bej.2020.107555" (2020)

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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4011",
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.
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. Molecular Diversity. 2020;24(3):593-601
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" 24, no. 3 (2020):593-601,
https://doi.org/10.1007/s11030-019-09965-0 .
2

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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4270",
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). Ekspresija, prečišćavanje i karakterizacija mutanata celobioza - dehidrogenaze iz Phanerochaete chrysosporium u Pichia pastoris KM71H soju.
Journal of the Serbian Chemical SocietyBelgrade : 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. Ekspresija, prečišćavanje i karakterizacija mutanata celobioza - dehidrogenaze iz Phanerochaete chrysosporium u Pichia pastoris KM71H soju. Journal of the Serbian Chemical Society. 2020;85(1):25-35
Balaž Ana Marija, Blažić Marija, Popović Nikolina, Prodanović Olivera, Ostafe Raluca, Fischer Rainer, Prodanović Radivoje, "Ekspresija, prečišćavanje i karakterizacija mutanata celobioza - dehidrogenaze iz Phanerochaete chrysosporium u Pichia pastoris KM71H soju" 85, no. 1 (2020):25-35,
https://doi.org/10.2298/JSC190320058B .

Polymeric Nanocarriers of Drug Delivery Systems in Cancer Therapy

Avramović, Nataša; Mandić, Boris; Savić-Radojević, Ana; Simić, Tatjana

(2020)

TY  - JOUR
AU  - Avramović, Nataša
AU  - Mandić, Boris
AU  - Savić-Radojević, Ana
AU  - Simić, Tatjana
PY  - 2020
UR  - https://www.mdpi.com/1999-4923/12/4/298
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4021
AB  - Conventional chemotherapy is the most common therapeutic method for treating cancer by the application of small toxic molecules thatinteract with DNA and causecell death. Unfortunately, these chemotherapeutic agents are non-selective and can damage both cancer and healthy tissues, producing diverse side effects, andthey can have a short circulation half-life and limited targeting. Many synthetic polymers have found application as nanocarriers of intelligent drug delivery systems (DDSs). Their unique physicochemical properties allow them to carry drugs with high efficiency, specificallytarget cancer tissue and control drug release. In recent years, considerable efforts have been made to design smart nanoplatforms, including amphiphilic block copolymers, polymer-drug conjugates and in particular pH- and redox-stimuli-responsive nanoparticles (NPs). This review is focused on a new generation of polymer-based DDSs with specific chemical functionalities that improve their hydrophilicity, drug loading and cellular interactions.Recentlydesigned multifunctional DDSs used in cancer therapy are highlighted in this review.
T2  - Pharmaceutics
T2  - Pharmaceutics
T1  - Polymeric Nanocarriers of Drug Delivery Systems in Cancer Therapy
VL  - 12
IS  - 4
SP  - 298
DO  - 10.3390/pharmaceutics12040298
ER  - 
@article{
author = "Avramović, Nataša and Mandić, Boris and Savić-Radojević, Ana and Simić, Tatjana",
year = "2020",
url = "https://www.mdpi.com/1999-4923/12/4/298, http://cherry.chem.bg.ac.rs/handle/123456789/4021",
abstract = "Conventional chemotherapy is the most common therapeutic method for treating cancer by the application of small toxic molecules thatinteract with DNA and causecell death. Unfortunately, these chemotherapeutic agents are non-selective and can damage both cancer and healthy tissues, producing diverse side effects, andthey can have a short circulation half-life and limited targeting. Many synthetic polymers have found application as nanocarriers of intelligent drug delivery systems (DDSs). Their unique physicochemical properties allow them to carry drugs with high efficiency, specificallytarget cancer tissue and control drug release. In recent years, considerable efforts have been made to design smart nanoplatforms, including amphiphilic block copolymers, polymer-drug conjugates and in particular pH- and redox-stimuli-responsive nanoparticles (NPs). This review is focused on a new generation of polymer-based DDSs with specific chemical functionalities that improve their hydrophilicity, drug loading and cellular interactions.Recentlydesigned multifunctional DDSs used in cancer therapy are highlighted in this review.",
journal = "Pharmaceutics, Pharmaceutics",
title = "Polymeric Nanocarriers of Drug Delivery Systems in Cancer Therapy",
volume = "12",
number = "4",
pages = "298",
doi = "10.3390/pharmaceutics12040298"
}
Avramović, N., Mandić, B., Savić-Radojević, A.,& Simić, T. (2020). Polymeric Nanocarriers of Drug Delivery Systems in Cancer Therapy.
Pharmaceutics, 12(4), 298.
https://doi.org/10.3390/pharmaceutics12040298
Avramović N, Mandić B, Savić-Radojević A, Simić T. Polymeric Nanocarriers of Drug Delivery Systems in Cancer Therapy. Pharmaceutics. 2020;12(4):298
Avramović Nataša, Mandić Boris, Savić-Radojević Ana, Simić Tatjana, "Polymeric Nanocarriers of Drug Delivery Systems in Cancer Therapy" 12, no. 4 (2020):298,
https://doi.org/10.3390/pharmaceutics12040298 .
1
17
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Proteinski inženjering celobioza - dehidrogenaze iz Phanerochaete chrysosporium u cilju povećanja oksidativne stabilnosti za primenu u biokatalizi

Balaž, Ana Marija

(Универзитет у Београду, Хемијски факултет, 2019-12-06)

TY  - BOOK
AU  - Balaž, Ana Marija
PY  - 2019-12-06
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7704
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22916/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23928841
UR  - https://nardus.mpn.gov.rs/handle/123456789/17616
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4383
AB  - Celobioza – dehidrogenaza poreklom iz Phanerochaete chrysosporium, gljive bele truleži, pripada ekstracelularnim oksidoredukcionim enzimima i katalizuje oksidaciju β – 1,4 – glikozidno vezanih oligosaharida poput celobioze i laktoze. Oksidacijom laktoze dolazi do formiranja laktobionske kiseline koja pronalazi veliku primenu u farmaceutskoj i kozmetičkoj industriji gde se koristi prilikom distribucije lekova i za hidrataciju kože kao sastavni deo različitih krema, gde zajedno sa hijaluronskom kiselinu ima ulogu u smanjenju bora.Celobioza – dehidrogenaza prilikom oksidacije laktoze ili celobioze, kao prirodnih supstrata, katalizuje redukciju jednog dvoelektronskog ili dva jednoelektronska akceptora elektrona. Jedan od najkorišćenijih dvoelektronskih akceptora elektrona je upravo dihlor fenol indofenol (DCIP), dok jednoelektronski akceptori elektrona mogu biti citohrom c, ABTS, ali i Fe3+ i Mn3+ joni. Redukcijom Fe3+ jona u prisustvu molekulskog kiseonika dolazi do formiranja vodonik peroksida i posredstvom Fentonove reakcije do generisanja hidroksil radikala.Polazeći od ove činjenice, iskoristili smo upravo Fentonovu reakciju za razvoj fluorescentnog eseja za visoko efikasnu pretragu biblioteka gena celobioza – dehidrogenaze, baziranog na detekciji proizvedenih hidroksil radikala fluorogenom probom aminofenil – fluoresceinom (APF).Primena celobioza – dehidrogenaze u konstruisanju biosenzora i biogorivnih ćelija leži upravo u njenoj sposobnosti da katalizuje oksidaciju laktoze, celobioze i β – 1,4 – vezanih oligosaharida do odgovarajućih laktona koji potom spontano hidrolizuju do aldonskih kiselina. Enzimi koji nalaze primenu u konstruisanju biosenzora i biogorivnih ćelija, moraju da zadovoljavaju nekoliko kriterijuma,odnosno moraju da imaju veliku osetljivost i supstratnu specifičnost, ali i da pokazuju povećanu stabilnost...
AB  - Cellobiose dehydrogenase from Phanerochaete chrysosporium, a white rot fungus, belongs to the extracellular oxidoreductive group of enzymes and catalyzes the oxidation of the β – 1,4 – glycoside bond of oligosaccharides such as cellobiose and lactose. During oxidation of lactose, formation of lactobionic acid occurs which has many applications in pharmaceutical and cosmetic industry. Such applications include the distribution of medicine, a component responsible for skin hydration and when combined with hyaluronic acid as an agent against wrinkles.During oxidation of lactose or cellobiose by cellobiose dehydrogenase, reduction catalysis occurs of one two electron or two one electron acceptors. One of the most utilized two electron acceptors is DCIP, while one electron acceptors are usually cytochrome c, ABTS, Fe3+ and Mn3+ ions. During reduction of Fe3+ ions in the presence of molecular oxygen, H2O2 is formed and due to the Fenton reaction formation of hydroxyl radicals occurs. Due to this occurrence we wanted to use the Fenton reaction in order to develop a fluorescent assay based on the production of hydroxyl radicals and the fluorescence of aminophenyl fluorescein (APF). This would allow us to efficiently analyze cellobiose dehydrogenase gene libraries.With this fact in mind, the Fenton reaction was used to develop a fluorescent assay for the high throughput screening of cellobiose dehydrogenase genes, based on the detection of hydroxyl radicals with the fluorescent probe APF.The possible application of cellobiose dehydrogenase in the construction of various biosensors and biofuel cells is due the its ability to catalyze the oxidation of lactose, cellobiose and similar β – 1,4 – oligosaccharides do their corresponding lactones which then spontaneously hydrolyze to aldonic acids. Enzymes used in suchapplications need to satisfy certain criteria, such as exceptional sensitivity, substrate selectivity, stability and activity...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Proteinski inženjering celobioza - dehidrogenaze iz Phanerochaete chrysosporium u cilju povećanja oksidativne stabilnosti za primenu u biokatalizi
ER  - 
@phdthesis{
author = "Balaž, Ana Marija",
year = "2019-12-06",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=7704, https://fedorabg.bg.ac.rs/fedora/get/o:22916/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23928841, https://nardus.mpn.gov.rs/handle/123456789/17616, http://cherry.chem.bg.ac.rs/handle/123456789/4383",
abstract = "Celobioza – dehidrogenaza poreklom iz Phanerochaete chrysosporium, gljive bele truleži, pripada ekstracelularnim oksidoredukcionim enzimima i katalizuje oksidaciju β – 1,4 – glikozidno vezanih oligosaharida poput celobioze i laktoze. Oksidacijom laktoze dolazi do formiranja laktobionske kiseline koja pronalazi veliku primenu u farmaceutskoj i kozmetičkoj industriji gde se koristi prilikom distribucije lekova i za hidrataciju kože kao sastavni deo različitih krema, gde zajedno sa hijaluronskom kiselinu ima ulogu u smanjenju bora.Celobioza – dehidrogenaza prilikom oksidacije laktoze ili celobioze, kao prirodnih supstrata, katalizuje redukciju jednog dvoelektronskog ili dva jednoelektronska akceptora elektrona. Jedan od najkorišćenijih dvoelektronskih akceptora elektrona je upravo dihlor fenol indofenol (DCIP), dok jednoelektronski akceptori elektrona mogu biti citohrom c, ABTS, ali i Fe3+ i Mn3+ joni. Redukcijom Fe3+ jona u prisustvu molekulskog kiseonika dolazi do formiranja vodonik peroksida i posredstvom Fentonove reakcije do generisanja hidroksil radikala.Polazeći od ove činjenice, iskoristili smo upravo Fentonovu reakciju za razvoj fluorescentnog eseja za visoko efikasnu pretragu biblioteka gena celobioza – dehidrogenaze, baziranog na detekciji proizvedenih hidroksil radikala fluorogenom probom aminofenil – fluoresceinom (APF).Primena celobioza – dehidrogenaze u konstruisanju biosenzora i biogorivnih ćelija leži upravo u njenoj sposobnosti da katalizuje oksidaciju laktoze, celobioze i β – 1,4 – vezanih oligosaharida do odgovarajućih laktona koji potom spontano hidrolizuju do aldonskih kiselina. Enzimi koji nalaze primenu u konstruisanju biosenzora i biogorivnih ćelija, moraju da zadovoljavaju nekoliko kriterijuma,odnosno moraju da imaju veliku osetljivost i supstratnu specifičnost, ali i da pokazuju povećanu stabilnost..., Cellobiose dehydrogenase from Phanerochaete chrysosporium, a white rot fungus, belongs to the extracellular oxidoreductive group of enzymes and catalyzes the oxidation of the β – 1,4 – glycoside bond of oligosaccharides such as cellobiose and lactose. During oxidation of lactose, formation of lactobionic acid occurs which has many applications in pharmaceutical and cosmetic industry. Such applications include the distribution of medicine, a component responsible for skin hydration and when combined with hyaluronic acid as an agent against wrinkles.During oxidation of lactose or cellobiose by cellobiose dehydrogenase, reduction catalysis occurs of one two electron or two one electron acceptors. One of the most utilized two electron acceptors is DCIP, while one electron acceptors are usually cytochrome c, ABTS, Fe3+ and Mn3+ ions. During reduction of Fe3+ ions in the presence of molecular oxygen, H2O2 is formed and due to the Fenton reaction formation of hydroxyl radicals occurs. Due to this occurrence we wanted to use the Fenton reaction in order to develop a fluorescent assay based on the production of hydroxyl radicals and the fluorescence of aminophenyl fluorescein (APF). This would allow us to efficiently analyze cellobiose dehydrogenase gene libraries.With this fact in mind, the Fenton reaction was used to develop a fluorescent assay for the high throughput screening of cellobiose dehydrogenase genes, based on the detection of hydroxyl radicals with the fluorescent probe APF.The possible application of cellobiose dehydrogenase in the construction of various biosensors and biofuel cells is due the its ability to catalyze the oxidation of lactose, cellobiose and similar β – 1,4 – oligosaccharides do their corresponding lactones which then spontaneously hydrolyze to aldonic acids. Enzymes used in suchapplications need to satisfy certain criteria, such as exceptional sensitivity, substrate selectivity, stability and activity...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Proteinski inženjering celobioza - dehidrogenaze iz Phanerochaete chrysosporium u cilju povećanja oksidativne stabilnosti za primenu u biokatalizi"
}
Balaž, A. M. (2019-12-06). Proteinski inženjering celobioza - dehidrogenaze iz Phanerochaete chrysosporium u cilju povećanja oksidativne stabilnosti za primenu u biokatalizi.
Универзитет у БеоградуУниверзитет у Београду, Хемијски факултет..
Balaž AM. Proteinski inženjering celobioza - dehidrogenaze iz Phanerochaete chrysosporium u cilju povećanja oksidativne stabilnosti za primenu u biokatalizi. Универзитет у Београду. 2019;
Balaž Ana Marija, "Proteinski inženjering celobioza - dehidrogenaze iz Phanerochaete chrysosporium u cilju povećanja oksidativne stabilnosti za primenu u biokatalizi" (2019-12-06)

Volatile composition, colour, and sensory quality of spirit-based beverages enriched with Medicinal Fungus Ganoderma lucidum and Herbal Extract

Veljović, Sonja P.; Tomić, Nikola S.; Belović, Miona M.; Nikićević, Ninoslav; Vukosavljević, Predrag V.; Nikšić, Miomir P.; Tešević, Vele

(University of Zagreb, 2019)

TY  - JOUR
AU  - Veljović, Sonja P.
AU  - Tomić, Nikola S.
AU  - Belović, Miona M.
AU  - Nikićević, Ninoslav
AU  - Vukosavljević, Predrag V.
AU  - Nikšić, Miomir P.
AU  - Tešević, Vele
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3681
AB  - The multicomponent mixtures consisting of herbs and fungi are commonly used for the production of alcoholic beverages with potential health-promoting effects in many Asian countries. The medicinal fungus Ganoderma lucidum is one of the most important fungi used for spirit production. Although this fungus affects the aromatic complexity of spirits, only a small number of studies have focused on investigating the influence of G. lucidum on the aromatic profile and colour of spirits. The aim of the research is to evaluate the influence of adding G. lucidum and herbal extract on final concentrations of volatile compounds and sensory quality of several distillates. In this study, distillates (grain, plum, grape and wine) were used to produce new spirit-based beverages with the fungus G. lucidum only, or with the fungus and herbal extract. Fifty-nine aroma compounds were identified by GC-MS. The aromatic profiles were strongly influenced by the primary aromas of the distillates, but the addition of G. lucidum and herbal extract enriched the volatile fraction of distillates with a range of ethyl esters, with a fruity and floral fragrance. Higher alcohols, 1-propanol, 2-isobutanol and isoamyl alcohol, were the most abundant volatile compounds in the analyzed distillates and spirits. The lightness of distillates was from 60.7 to 63.6, and with the addition of Ganoderma it significantly decreased to the range from 43.6 to 50.5. The addition of the fungus also increased the intensity of red and yellow colours. The Ganoderma spirits scored very highly in sensory evaluation (17.6-18.3), significantly better than the spirits without any additions (16.1-16.9).
PB  - University of Zagreb
T2  - Food Technology and Biotechnology
T1  - Volatile composition, colour, and sensory quality of spirit-based beverages enriched with Medicinal Fungus Ganoderma lucidum and Herbal Extract
VL  - 57
IS  - 3
SP  - 408
EP  - 417
DO  - 10.17113/ftb.57.03.19.6106
ER  - 
@article{
author = "Veljović, Sonja P. and Tomić, Nikola S. and Belović, Miona M. and Nikićević, Ninoslav and Vukosavljević, Predrag V. and Nikšić, Miomir P. and Tešević, Vele",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3681",
abstract = "The multicomponent mixtures consisting of herbs and fungi are commonly used for the production of alcoholic beverages with potential health-promoting effects in many Asian countries. The medicinal fungus Ganoderma lucidum is one of the most important fungi used for spirit production. Although this fungus affects the aromatic complexity of spirits, only a small number of studies have focused on investigating the influence of G. lucidum on the aromatic profile and colour of spirits. The aim of the research is to evaluate the influence of adding G. lucidum and herbal extract on final concentrations of volatile compounds and sensory quality of several distillates. In this study, distillates (grain, plum, grape and wine) were used to produce new spirit-based beverages with the fungus G. lucidum only, or with the fungus and herbal extract. Fifty-nine aroma compounds were identified by GC-MS. The aromatic profiles were strongly influenced by the primary aromas of the distillates, but the addition of G. lucidum and herbal extract enriched the volatile fraction of distillates with a range of ethyl esters, with a fruity and floral fragrance. Higher alcohols, 1-propanol, 2-isobutanol and isoamyl alcohol, were the most abundant volatile compounds in the analyzed distillates and spirits. The lightness of distillates was from 60.7 to 63.6, and with the addition of Ganoderma it significantly decreased to the range from 43.6 to 50.5. The addition of the fungus also increased the intensity of red and yellow colours. The Ganoderma spirits scored very highly in sensory evaluation (17.6-18.3), significantly better than the spirits without any additions (16.1-16.9).",
publisher = "University of Zagreb",
journal = "Food Technology and Biotechnology",
title = "Volatile composition, colour, and sensory quality of spirit-based beverages enriched with Medicinal Fungus Ganoderma lucidum and Herbal Extract",
volume = "57",
number = "3",
pages = "408-417",
doi = "10.17113/ftb.57.03.19.6106"
}
Veljović, S. P., Tomić, N. S., Belović, M. M., Nikićević, N., Vukosavljević, P. V., Nikšić, M. P.,& Tešević, V. (2019). Volatile composition, colour, and sensory quality of spirit-based beverages enriched with Medicinal Fungus Ganoderma lucidum and Herbal Extract.
Food Technology and BiotechnologyUniversity of Zagreb., 57(3), 408-417.
https://doi.org/10.17113/ftb.57.03.19.6106
Veljović SP, Tomić NS, Belović MM, Nikićević N, Vukosavljević PV, Nikšić MP, Tešević V. Volatile composition, colour, and sensory quality of spirit-based beverages enriched with Medicinal Fungus Ganoderma lucidum and Herbal Extract. Food Technology and Biotechnology. 2019;57(3):408-417
Veljović Sonja P., Tomić Nikola S., Belović Miona M., Nikićević Ninoslav, Vukosavljević Predrag V., Nikšić Miomir P., Tešević Vele, "Volatile composition, colour, and sensory quality of spirit-based beverages enriched with Medicinal Fungus Ganoderma lucidum and Herbal Extract" 57, no. 3 (2019):408-417,
https://doi.org/10.17113/ftb.57.03.19.6106 .
3
2
3

Application of polyphenol-loaded nanoparticles in food industry

Milinčić, Danijel D.; Popović, Dušanka A.; Lević, Steva M.; Kostić, Aleksandar Ž.; Tešić, Živoslav Lj.; Nedović, Viktor A.; Pešić, Mirjana B.

(MDPI, 2019)

TY  - JOUR
AU  - Milinčić, Danijel D.
AU  - Popović, Dušanka A.
AU  - Lević, Steva M.
AU  - Kostić, Aleksandar Ž.
AU  - Tešić, Živoslav Lj.
AU  - Nedović, Viktor A.
AU  - Pešić, Mirjana B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3780
AB  - Nanotechnology is an emerging field of science, and nanotechnological concepts have been intensively studied for potential applications in the food industry. Nanoparticles (with dimensions ranging from one to several hundred nanometers) have specific characteristics and better functionality, thanks to their size and other physicochemical properties. Polyphenols are recognized as active compounds that have several putative beneficial properties, including antioxidant, antimicrobial, and anticancer activity. However, the use of polyphenols as functional food ingredients faces numerous challenges, such as their poor stability, solubility, and bioavailability. These difficulties could be solved relatively easily by the application of encapsulation. The objective of this review is to present the most recent accomplishments in the usage of polyphenol-loaded nanoparticles in food science. Nanoparticles loaded with polyphenols and their applications as active ingredients for improving physicochemical and functional properties of food, or as components of active packaging materials, were critically reviewed. Potential adverse effects of polyphenol-loaded nanomaterials are also discussed.
PB  - MDPI
T2  - Nanomaterials
T1  - Application of polyphenol-loaded nanoparticles in food industry
VL  - 9
IS  - 11
SP  - 1629
DO  - 10.3390/nano9111629
ER  - 
@article{
author = "Milinčić, Danijel D. and Popović, Dušanka A. and Lević, Steva M. and Kostić, Aleksandar Ž. and Tešić, Živoslav Lj. and Nedović, Viktor A. and Pešić, Mirjana B.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3780",
abstract = "Nanotechnology is an emerging field of science, and nanotechnological concepts have been intensively studied for potential applications in the food industry. Nanoparticles (with dimensions ranging from one to several hundred nanometers) have specific characteristics and better functionality, thanks to their size and other physicochemical properties. Polyphenols are recognized as active compounds that have several putative beneficial properties, including antioxidant, antimicrobial, and anticancer activity. However, the use of polyphenols as functional food ingredients faces numerous challenges, such as their poor stability, solubility, and bioavailability. These difficulties could be solved relatively easily by the application of encapsulation. The objective of this review is to present the most recent accomplishments in the usage of polyphenol-loaded nanoparticles in food science. Nanoparticles loaded with polyphenols and their applications as active ingredients for improving physicochemical and functional properties of food, or as components of active packaging materials, were critically reviewed. Potential adverse effects of polyphenol-loaded nanomaterials are also discussed.",
publisher = "MDPI",
journal = "Nanomaterials",
title = "Application of polyphenol-loaded nanoparticles in food industry",
volume = "9",
number = "11",
pages = "1629",
doi = "10.3390/nano9111629"
}
Milinčić, D. D., Popović, D. A., Lević, S. M., Kostić, A. Ž., Tešić, Ž. Lj., Nedović, V. A.,& Pešić, M. B. (2019). Application of polyphenol-loaded nanoparticles in food industry.
NanomaterialsMDPI., 9(11), 1629.
https://doi.org/10.3390/nano9111629
Milinčić DD, Popović DA, Lević SM, Kostić AŽ, Tešić ŽL, Nedović VA, Pešić MB. Application of polyphenol-loaded nanoparticles in food industry. Nanomaterials. 2019;9(11):1629
Milinčić Danijel D., Popović Dušanka A., Lević Steva M., Kostić Aleksandar Ž., Tešić Živoslav Lj., Nedović Viktor A., Pešić Mirjana B., "Application of polyphenol-loaded nanoparticles in food industry" 9, no. 11 (2019):1629,
https://doi.org/10.3390/nano9111629 .
20
11
17

Mycotoxins and mycotoxin producing fungi in pollen: Review

Kostić, Aleksandar Ž.; Milinčić, Danijel D.; Petrović, Tanja S.; Krnjaja, Vesna S.; Stanojević, Slađana P.; Barać, Miroljub B.; Tešić, Živoslav Lj.; Pešić, Mirjana B.

(MDPI, 2019)

TY  - JOUR
AU  - Kostić, Aleksandar Ž.
AU  - Milinčić, Danijel D.
AU  - Petrović, Tanja S.
AU  - Krnjaja, Vesna S.
AU  - Stanojević, Slađana P.
AU  - Barać, Miroljub B.
AU  - Tešić, Živoslav Lj.
AU  - Pešić, Mirjana B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2837
AB  - Due to its divergent chemical composition and good nutritional properties, pollen is not only important as a potential food supplement but also as a good substrate for the development of different microorganisms. Among such microorganisms, toxigenic fungi are extremely dangerous as they can synthesize mycotoxins as a part of their metabolic pathways. Furthermore, favorable conditions that enable the synthesis of mycotoxins (adequate temperature, relative humidity, pH, and a w values) are found frequently during pollen collection and/or production process. Internationally, several different mycotoxins have been identified in pollen samples, with a noted predominance of aflatoxins, ochratoxins, fumonisins, zearalenone, deoxynivalenol, and T-2 toxin. Mycotoxins are, generally speaking, extremely harmful for humans and other mammals. Current EU legislation contains guidelines on the permissible content of this group of compounds, but without information pertaining to the content of mycotoxins in pollen. Currently only aflatoxins have been researched and discussed in the literature in regard to proposed limits. Therefore, the aim of this review is to give information about the presence of different mycotoxins in pollen samples collected all around the world, to propose possible aflatoxin contamination pathways, and to emphasize the importance of a regular mycotoxicological analysis of pollen. Furthermore, a suggestion is made regarding the legal regulation of pollen as a food supplement and the proposed tolerable limits for other mycotoxins.
PB  - MDPI
T2  - Toxins
T1  - Mycotoxins and mycotoxin producing fungi in pollen: Review
VL  - 11
IS  - 2
SP  - 1
EP  - 20
DO  - 10.3390/toxins11020064
ER  - 
@article{
author = "Kostić, Aleksandar Ž. and Milinčić, Danijel D. and Petrović, Tanja S. and Krnjaja, Vesna S. and Stanojević, Slađana P. and Barać, Miroljub B. and Tešić, Živoslav Lj. and Pešić, Mirjana B.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2837",
abstract = "Due to its divergent chemical composition and good nutritional properties, pollen is not only important as a potential food supplement but also as a good substrate for the development of different microorganisms. Among such microorganisms, toxigenic fungi are extremely dangerous as they can synthesize mycotoxins as a part of their metabolic pathways. Furthermore, favorable conditions that enable the synthesis of mycotoxins (adequate temperature, relative humidity, pH, and a w values) are found frequently during pollen collection and/or production process. Internationally, several different mycotoxins have been identified in pollen samples, with a noted predominance of aflatoxins, ochratoxins, fumonisins, zearalenone, deoxynivalenol, and T-2 toxin. Mycotoxins are, generally speaking, extremely harmful for humans and other mammals. Current EU legislation contains guidelines on the permissible content of this group of compounds, but without information pertaining to the content of mycotoxins in pollen. Currently only aflatoxins have been researched and discussed in the literature in regard to proposed limits. Therefore, the aim of this review is to give information about the presence of different mycotoxins in pollen samples collected all around the world, to propose possible aflatoxin contamination pathways, and to emphasize the importance of a regular mycotoxicological analysis of pollen. Furthermore, a suggestion is made regarding the legal regulation of pollen as a food supplement and the proposed tolerable limits for other mycotoxins.",
publisher = "MDPI",
journal = "Toxins",
title = "Mycotoxins and mycotoxin producing fungi in pollen: Review",
volume = "11",
number = "2",
pages = "1-20",
doi = "10.3390/toxins11020064"
}
Kostić, A. Ž., Milinčić, D. D., Petrović, T. S., Krnjaja, V. S., Stanojević, S. P., Barać, M. B., Tešić, Ž. Lj.,& Pešić, M. B. (2019). Mycotoxins and mycotoxin producing fungi in pollen: Review.
ToxinsMDPI., 11(2), 1-20.
https://doi.org/10.3390/toxins11020064
Kostić AŽ, Milinčić DD, Petrović TS, Krnjaja VS, Stanojević SP, Barać MB, Tešić ŽL, Pešić MB. Mycotoxins and mycotoxin producing fungi in pollen: Review. Toxins. 2019;11(2):1-20
Kostić Aleksandar Ž., Milinčić Danijel D., Petrović Tanja S., Krnjaja Vesna S., Stanojević Slađana P., Barać Miroljub B., Tešić Živoslav Lj., Pešić Mirjana B., "Mycotoxins and mycotoxin producing fungi in pollen: Review" 11, no. 2 (2019):1-20,
https://doi.org/10.3390/toxins11020064 .
10
7
10

Platinum and ruthenium complexes as promising molecules in cancer therapy

Avramović, Nataša; Ignjatović, Nikola; Savić, Aleksandar

(Srpsko lekarsko društvo, 2019)

TY  - JOUR
AU  - Avramović, Nataša
AU  - Ignjatović, Nikola
AU  - Savić, Aleksandar
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3304
AB  - Cancer is one of the most common fatal diseases in humans nowadays. About 20 million new cancer cases are expected in the next two decades worldwide. The development of new chemotherapeutic agents with improved properties is presently the main challenge in the medicinal chemistry. Cisplatin was introduced to oncology in 1978 as first chemotherapeutic agent regarding its specific interaction with DNA, leading to its damage and causing the cell death. Since the first application of cisplatin in cancer therapy, there has been a growing interest in new metal-based compounds, in particular platinum and ruthenium complexes, with better anticancer activity and less side-effects compared to cisplatin. Carboplatin and oxaliplatin have shown promising action against some types of cancer, which are resistant to cisplatin. With the aim to overcome cross-resistance to these Pt(II) drugs, bioavailable platinum complexes (satraplatin and picoplatin) firstly found application as orally administered drugs, as well as some combined therapies of Pt(II) drugs (cisplatin, picoplatin) with specific resistant modulators. In recent years, novel polymer and liposomal formulations of platinum drugs (prolindac, lipoplatin, lipoxal, aroplatin) have been designed with strategy to improve drug delivery to target cancer cells and reduce toxicity. Complexes based on ruthenium have great potential to become leading candidates for the medical use in anticancer therapy. Some of these compounds have shown good anticancer activity, both in vitro and in vivo and two of them (KP1019 and NAMI-A) have passed clinical trials and given promising results.
PB  - Srpsko lekarsko društvo
T2  - Srpski Arhiv za Celokupno Lekarstvo
T1  - Platinum and ruthenium complexes as promising molecules in cancer therapy
VL  - 147
IS  - 1-2
SP  - 105
EP  - 109
DO  - 10.2298/SARH180706075A
ER  - 
@article{
author = "Avramović, Nataša and Ignjatović, Nikola and Savić, Aleksandar",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3304",
abstract = "Cancer is one of the most common fatal diseases in humans nowadays. About 20 million new cancer cases are expected in the next two decades worldwide. The development of new chemotherapeutic agents with improved properties is presently the main challenge in the medicinal chemistry. Cisplatin was introduced to oncology in 1978 as first chemotherapeutic agent regarding its specific interaction with DNA, leading to its damage and causing the cell death. Since the first application of cisplatin in cancer therapy, there has been a growing interest in new metal-based compounds, in particular platinum and ruthenium complexes, with better anticancer activity and less side-effects compared to cisplatin. Carboplatin and oxaliplatin have shown promising action against some types of cancer, which are resistant to cisplatin. With the aim to overcome cross-resistance to these Pt(II) drugs, bioavailable platinum complexes (satraplatin and picoplatin) firstly found application as orally administered drugs, as well as some combined therapies of Pt(II) drugs (cisplatin, picoplatin) with specific resistant modulators. In recent years, novel polymer and liposomal formulations of platinum drugs (prolindac, lipoplatin, lipoxal, aroplatin) have been designed with strategy to improve drug delivery to target cancer cells and reduce toxicity. Complexes based on ruthenium have great potential to become leading candidates for the medical use in anticancer therapy. Some of these compounds have shown good anticancer activity, both in vitro and in vivo and two of them (KP1019 and NAMI-A) have passed clinical trials and given promising results.",
publisher = "Srpsko lekarsko društvo",
journal = "Srpski Arhiv za Celokupno Lekarstvo",
title = "Platinum and ruthenium complexes as promising molecules in cancer therapy",
volume = "147",
number = "1-2",
pages = "105-109",
doi = "10.2298/SARH180706075A"
}
Avramović, N., Ignjatović, N.,& Savić, A. (2019). Platinum and ruthenium complexes as promising molecules in cancer therapy.
Srpski Arhiv za Celokupno LekarstvoSrpsko lekarsko društvo., 147(1-2), 105-109.
https://doi.org/10.2298/SARH180706075A
Avramović N, Ignjatović N, Savić A. Platinum and ruthenium complexes as promising molecules in cancer therapy. Srpski Arhiv za Celokupno Lekarstvo. 2019;147(1-2):105-109
Avramović Nataša, Ignjatović Nikola, Savić Aleksandar, "Platinum and ruthenium complexes as promising molecules in cancer therapy" 147, no. 1-2 (2019):105-109,
https://doi.org/10.2298/SARH180706075A .
1
1
1

Enzymatic lipophilization of vitamin C with linoleic acid: Determination of antioxidant and diffusion properties of L-ascorbyl linoleate

Ćorović, Marija; Milivojević, Ana; Carević, Milica B.; Banjanac, Katarina; Vujisić, Ljubodrag V.; Pjanović, Rada V.; Bezbradica, Dejan

(2018)

TY  - JOUR
AU  - Ćorović, Marija
AU  - Milivojević, Ana
AU  - Carević, Milica B.
AU  - Banjanac, Katarina
AU  - Vujisić, Ljubodrag V.
AU  - Pjanović, Rada V.
AU  - Bezbradica, Dejan
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/217
AB  - Lipophilic derivatives of vitamin C are additives with antioxidant properties, attractive for application in food, cosmetics and pharmaceutics. They could be synthesized in lipase-catalyzed processes by using various acyl donors. Hereby, we present application of linoleic acid, which is polyunsaturated fatty acid essential in human nutrition, for esterification of vitamin C catalyzed by immobilized enzyme preparation Novozym® 435 in acetone. Highest specific ester yield, 9.7 mmol/g of immobilized lipase, was accomplished with 0.15 M of vitamin C, 0.6 M of linoleic acid, 3 g/l of enzyme and 0.07% (v/v) of water, at 60°C. NMR analyses of purified product proved that synthesized molecule was identical to 6-O-ascorbyl linoleate. Capacity of ester for scavenging 2,2-diphenyl-1-picrylhydrazyl radicals was two times higher comparing to parent molecule, vitamin C. Its diffusion coefficient, determined using Franz cell and cellulose acetate membrane, was 40% higher than palmitate and 62% higher than oleate. Obtained results showed that L-ascorbyl linoleate could be successfully synthesized in biocatalyzed processes. Furthermore, it was demonstrated that it possess high potential for application in different lipophilic products due to its liposolubility, high antioxidant efficiency and good diffusion properties.
AB  - Lipofilni derivati vitamina C su aditivi sa antioksidativnim dejstvom pogodni za primenu u prehrambenim, kozmetičkim i farmaceutskim proizvodima. Mogu biti sintetisani u procesima katalizovanim lipazama korišćenjem različitih acil-donora. U ovom radu, opisana je primena linolne kiseline, polinezasićene masne kiseline esencijalne u ljudskoj ishrani, u esterifikaciji vitamina C katalizovanoj imobilisanim enzimskim preparatom Novozym® 435 u acetonu. Najviši specifični prinos estra od 9,7 mmol/g imobilisane lipaze, ostvaren je sa 0,15 M vitamina C, 0,6 M linolne kiseline, 3 g/l enzima i 0,07 zapr. % vode, na 60°C. NMR analize prečišćenog proizvoda dokazale su da je sintetisani molekul identičan 6-O-askorbil-linolatu. Kapacitet estra za vezivanje 2,2- difenil-1-pikrilhidrazil radikala bio je dva puta viši u odnosu na sam vitamin C. Njegov koeficijent difuzije, određen korišćenjem Franz-ove ćelije i celuloza-acetatne membrane, bio je za 40% viši u odnosu na palmitat i za 62% u odnosu na oleat. Ostvareni rezultati pokazali su da L-askorbil-linolat može uspešno biti sintetisan u biokatalizovanom procesu. Pored toga, dokazano je da ovaj estar poseduje značajan potencijal za primenu u različitim lipofilnim proizvodima zbog svoje liposolubilnosti, snažnog antioksidativnog dejstva i pogodnih difuzionih karakteristika.
T2  - Food and Feed Research
T1  - Enzymatic lipophilization of vitamin C with linoleic acid: Determination of antioxidant and diffusion properties of L-ascorbyl linoleate
T1  - enzimska lipofilizacija vitamina C linolnom kiselinom - određivanje antioksidativnih i difuzionih svojstava L-askorbil-linolata
VL  - 45
IS  - 1
SP  - 1
EP  - 10
DO  - 10.5937/FFR1801001C
ER  - 
@article{
author = "Ćorović, Marija and Milivojević, Ana and Carević, Milica B. and Banjanac, Katarina and Vujisić, Ljubodrag V. and Pjanović, Rada V. and Bezbradica, Dejan",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/217",
abstract = "Lipophilic derivatives of vitamin C are additives with antioxidant properties, attractive for application in food, cosmetics and pharmaceutics. They could be synthesized in lipase-catalyzed processes by using various acyl donors. Hereby, we present application of linoleic acid, which is polyunsaturated fatty acid essential in human nutrition, for esterification of vitamin C catalyzed by immobilized enzyme preparation Novozym® 435 in acetone. Highest specific ester yield, 9.7 mmol/g of immobilized lipase, was accomplished with 0.15 M of vitamin C, 0.6 M of linoleic acid, 3 g/l of enzyme and 0.07% (v/v) of water, at 60°C. NMR analyses of purified product proved that synthesized molecule was identical to 6-O-ascorbyl linoleate. Capacity of ester for scavenging 2,2-diphenyl-1-picrylhydrazyl radicals was two times higher comparing to parent molecule, vitamin C. Its diffusion coefficient, determined using Franz cell and cellulose acetate membrane, was 40% higher than palmitate and 62% higher than oleate. Obtained results showed that L-ascorbyl linoleate could be successfully synthesized in biocatalyzed processes. Furthermore, it was demonstrated that it possess high potential for application in different lipophilic products due to its liposolubility, high antioxidant efficiency and good diffusion properties., Lipofilni derivati vitamina C su aditivi sa antioksidativnim dejstvom pogodni za primenu u prehrambenim, kozmetičkim i farmaceutskim proizvodima. Mogu biti sintetisani u procesima katalizovanim lipazama korišćenjem različitih acil-donora. U ovom radu, opisana je primena linolne kiseline, polinezasićene masne kiseline esencijalne u ljudskoj ishrani, u esterifikaciji vitamina C katalizovanoj imobilisanim enzimskim preparatom Novozym® 435 u acetonu. Najviši specifični prinos estra od 9,7 mmol/g imobilisane lipaze, ostvaren je sa 0,15 M vitamina C, 0,6 M linolne kiseline, 3 g/l enzima i 0,07 zapr. % vode, na 60°C. NMR analize prečišćenog proizvoda dokazale su da je sintetisani molekul identičan 6-O-askorbil-linolatu. Kapacitet estra za vezivanje 2,2- difenil-1-pikrilhidrazil radikala bio je dva puta viši u odnosu na sam vitamin C. Njegov koeficijent difuzije, određen korišćenjem Franz-ove ćelije i celuloza-acetatne membrane, bio je za 40% viši u odnosu na palmitat i za 62% u odnosu na oleat. Ostvareni rezultati pokazali su da L-askorbil-linolat može uspešno biti sintetisan u biokatalizovanom procesu. Pored toga, dokazano je da ovaj estar poseduje značajan potencijal za primenu u različitim lipofilnim proizvodima zbog svoje liposolubilnosti, snažnog antioksidativnog dejstva i pogodnih difuzionih karakteristika.",
journal = "Food and Feed Research",
title = "Enzymatic lipophilization of vitamin C with linoleic acid: Determination of antioxidant and diffusion properties of L-ascorbyl linoleate, enzimska lipofilizacija vitamina C linolnom kiselinom - određivanje antioksidativnih i difuzionih svojstava L-askorbil-linolata",
volume = "45",
number = "1",
pages = "1-10",
doi = "10.5937/FFR1801001C"
}
Ćorović, M., Milivojević, A., Carević, M. B., Banjanac, K., Vujisić, L. V., Pjanović, R. V.,& Bezbradica, D. (2018). enzimska lipofilizacija vitamina C linolnom kiselinom - određivanje antioksidativnih i difuzionih svojstava L-askorbil-linolata.
Food and Feed Research, 45(1), 1-10.
https://doi.org/10.5937/FFR1801001C
Ćorović M, Milivojević A, Carević MB, Banjanac K, Vujisić LV, Pjanović RV, Bezbradica D. enzimska lipofilizacija vitamina C linolnom kiselinom - određivanje antioksidativnih i difuzionih svojstava L-askorbil-linolata. Food and Feed Research. 2018;45(1):1-10
Ćorović Marija, Milivojević Ana, Carević Milica B., Banjanac Katarina, Vujisić Ljubodrag V., Pjanović Rada V., Bezbradica Dejan, "enzimska lipofilizacija vitamina C linolnom kiselinom - određivanje antioksidativnih i difuzionih svojstava L-askorbil-linolata" 45, no. 1 (2018):1-10,
https://doi.org/10.5937/FFR1801001C .

Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases

Trbojević-Ivić, Jovana; Milosavić, Nenad; Dimitrijević, Aleksandra; Gavrović-Jankulović, Marija; Bezbradica, Dejan; Kolarski, Dušan; Veličković, Dušan

(Elsevier Sci Ltd, Oxford, 2017)

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Milosavić, Nenad
AU  - Dimitrijević, Aleksandra
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Kolarski, Dušan
AU  - Veličković, Dušan
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3102
AB  - A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases
VL  - 218
SP  - 505
EP  - 508
DO  - 10.1016/j.foodchem.2016.09.049
ER  - 
@article{
author = "Trbojević-Ivić, Jovana and Milosavić, Nenad and Dimitrijević, Aleksandra and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Kolarski, Dušan and Veličković, Dušan",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3102",
abstract = "A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases",
volume = "218",
pages = "505-508",
doi = "10.1016/j.foodchem.2016.09.049"
}
Trbojević-Ivić, J., Milosavić, N., Dimitrijević, A., Gavrović-Jankulović, M., Bezbradica, D., Kolarski, D.,& Veličković, D. (2017). Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases.
Food ChemistryElsevier Sci Ltd, Oxford., 218, 505-508.
https://doi.org/10.1016/j.foodchem.2016.09.049
Trbojević-Ivić J, Milosavić N, Dimitrijević A, Gavrović-Jankulović M, Bezbradica D, Kolarski D, Veličković D. Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. Food Chemistry. 2017;218:505-508
Trbojević-Ivić Jovana, Milosavić Nenad, Dimitrijević Aleksandra, Gavrović-Jankulović Marija, Bezbradica Dejan, Kolarski Dušan, Veličković Dušan, "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases" 218 (2017):505-508,
https://doi.org/10.1016/j.foodchem.2016.09.049 .
12
8
9

Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation

Milivojević, Ana; Ćorović, Marija; Carević, Milica; Banjanac, Katarina; Vujisić, Ljubodrag V.; Veličković, Dusan; Bezbradica, Dejan

(Elsevier Science Bv, Amsterdam, 2017)

TY  - JOUR
AU  - Milivojević, Ana
AU  - Ćorović, Marija
AU  - Carević, Milica
AU  - Banjanac, Katarina
AU  - Vujisić, Ljubodrag V.
AU  - Veličković, Dusan
AU  - Bezbradica, Dejan
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2558
AB  - Solubility and stability of flavonoid glycosides, valuable natural constituents of cosmetics and pharmaceuticals, could be improved by lipase-catalyzed acylation. Focus of this study was on development of eco-friendly process for the production of flavonoid acetates. By using phloridzin as model compound and triacetin as acetyl donor and solvent, 100% conversion and high productivity (23.32 gl(-1) day(-1)) were accomplished. Complete conversions of two other glycosylated flavonoids, naringin and esculin, in solvent-free system were achieved, as well. Comprehensive kinetic mechanism based on two con-secutive mono-substrate reactions was established where first one represents formation of flavonoid monoacetate and within second reaction diacetate is being produced from monoacetate. Both steps were regarded as reversible Michaelis-Menten reactions without inhibition. Apparent kinetic parameters for two consecutive reactions (V-m constants for substrates and products and Km constants for forward and reverse reactions) were estimated for three examined acetyl acceptors and excellent fitting of experimental data (R-2 gt 0.97) was achieved. Obtained results showed that derived kinetic model could be applicable for solvent-free esterifications of different flavonoid glycosides. It was valid for entire transesterification course (72 h of reaction) which, combined with complete conversions and green character of synthesis, represents firm basis for further process development. (C) 2017 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation
VL  - 128
SP  - 106
EP  - 115
DO  - 10.1016/j.bej.2017.09.018
ER  - 
@article{
author = "Milivojević, Ana and Ćorović, Marija and Carević, Milica and Banjanac, Katarina and Vujisić, Ljubodrag V. and Veličković, Dusan and Bezbradica, Dejan",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2558",
abstract = "Solubility and stability of flavonoid glycosides, valuable natural constituents of cosmetics and pharmaceuticals, could be improved by lipase-catalyzed acylation. Focus of this study was on development of eco-friendly process for the production of flavonoid acetates. By using phloridzin as model compound and triacetin as acetyl donor and solvent, 100% conversion and high productivity (23.32 gl(-1) day(-1)) were accomplished. Complete conversions of two other glycosylated flavonoids, naringin and esculin, in solvent-free system were achieved, as well. Comprehensive kinetic mechanism based on two con-secutive mono-substrate reactions was established where first one represents formation of flavonoid monoacetate and within second reaction diacetate is being produced from monoacetate. Both steps were regarded as reversible Michaelis-Menten reactions without inhibition. Apparent kinetic parameters for two consecutive reactions (V-m constants for substrates and products and Km constants for forward and reverse reactions) were estimated for three examined acetyl acceptors and excellent fitting of experimental data (R-2 gt 0.97) was achieved. Obtained results showed that derived kinetic model could be applicable for solvent-free esterifications of different flavonoid glycosides. It was valid for entire transesterification course (72 h of reaction) which, combined with complete conversions and green character of synthesis, represents firm basis for further process development. (C) 2017 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation",
volume = "128",
pages = "106-115",
doi = "10.1016/j.bej.2017.09.018"
}
Milivojević, A., Ćorović, M., Carević, M., Banjanac, K., Vujisić, L. V., Veličković, D.,& Bezbradica, D. (2017). Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation.
Biochemical Engineering JournalElsevier Science Bv, Amsterdam., 128, 106-115.
https://doi.org/10.1016/j.bej.2017.09.018
Milivojević A, Ćorović M, Carević M, Banjanac K, Vujisić LV, Veličković D, Bezbradica D. Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation. Biochemical Engineering Journal. 2017;128:106-115
Milivojević Ana, Ćorović Marija, Carević Milica, Banjanac Katarina, Vujisić Ljubodrag V., Veličković Dusan, Bezbradica Dejan, "Highly efficient enzymatic acetylation of flavonoids: Development of solvent-free process and kinetic evaluation" 128 (2017):106-115,
https://doi.org/10.1016/j.bej.2017.09.018 .
5
5
5

Supplementary data for article: Milivojević, A.; Ćorović, M.; Carevic, M.; Banjanac, K.; Vujisić, L. V.; Velickovic, D.; Bezbradica, D. Highly Efficient Enzymatic Acetylation of Flavonoids: Development of Solvent-Free Process and Kinetic Evaluation. Biochemical Engineering Journal 2017, 128, 106–115. https://doi.org/10.1016/j.bej.2017.09.018.

Milivojević, Ana; Ćorović, Marija; Carević, Milica; Banjanac, Katarina; Vujisić, Ljubodrag V.; Veličković, Dusan; Bezbradica, Dejan

(Elsevier Science Bv, Amsterdam, 2017)

TY  - BOOK
AU  - Milivojević, Ana
AU  - Ćorović, Marija
AU  - Carević, Milica
AU  - Banjanac, Katarina
AU  - Vujisić, Ljubodrag V.
AU  - Veličković, Dusan
AU  - Bezbradica, Dejan
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2974
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Supplementary data for article: Milivojević, A.; Ćorović, M.; Carevic, M.; Banjanac, K.; Vujisić, L. V.; Velickovic, D.; Bezbradica, D. Highly Efficient Enzymatic Acetylation of Flavonoids: Development of Solvent-Free Process and Kinetic Evaluation. Biochemical Engineering Journal 2017, 128, 106–115. https://doi.org/10.1016/j.bej.2017.09.018.
ER  - 
@book{
author = "Milivojević, Ana and Ćorović, Marija and Carević, Milica and Banjanac, Katarina and Vujisić, Ljubodrag V. and Veličković, Dusan and Bezbradica, Dejan",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2974",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Supplementary data for article: Milivojević, A.; Ćorović, M.; Carevic, M.; Banjanac, K.; Vujisić, L. V.; Velickovic, D.; Bezbradica, D. Highly Efficient Enzymatic Acetylation of Flavonoids: Development of Solvent-Free Process and Kinetic Evaluation. Biochemical Engineering Journal 2017, 128, 106–115. https://doi.org/10.1016/j.bej.2017.09.018."
}
Milivojević, A., Ćorović, M., Carević, M., Banjanac, K., Vujisić, L. V., Veličković, D.,& Bezbradica, D. (2017). Supplementary data for article: Milivojević, A.; Ćorović, M.; Carevic, M.; Banjanac, K.; Vujisić, L. V.; Velickovic, D.; Bezbradica, D. Highly Efficient Enzymatic Acetylation of Flavonoids: Development of Solvent-Free Process and Kinetic Evaluation. Biochemical Engineering Journal 2017, 128, 106–115. https://doi.org/10.1016/j.bej.2017.09.018..
Biochemical Engineering JournalElsevier Science Bv, Amsterdam..
Milivojević A, Ćorović M, Carević M, Banjanac K, Vujisić LV, Veličković D, Bezbradica D. Supplementary data for article: Milivojević, A.; Ćorović, M.; Carevic, M.; Banjanac, K.; Vujisić, L. V.; Velickovic, D.; Bezbradica, D. Highly Efficient Enzymatic Acetylation of Flavonoids: Development of Solvent-Free Process and Kinetic Evaluation. Biochemical Engineering Journal 2017, 128, 106–115. https://doi.org/10.1016/j.bej.2017.09.018.. Biochemical Engineering Journal. 2017;
Milivojević Ana, Ćorović Marija, Carević Milica, Banjanac Katarina, Vujisić Ljubodrag V., Veličković Dusan, Bezbradica Dejan, "Supplementary data for article: Milivojević, A.; Ćorović, M.; Carevic, M.; Banjanac, K.; Vujisić, L. V.; Velickovic, D.; Bezbradica, D. Highly Efficient Enzymatic Acetylation of Flavonoids: Development of Solvent-Free Process and Kinetic Evaluation. Biochemical Engineering Journal 2017, 128, 106–115. https://doi.org/10.1016/j.bej.2017.09.018." (2017)

Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases

Trbojević-Ivić, Jovana; Milosavić, Nenad; Dimitrijević, Aleksandra; Gavrović-Jankulović, Marija; Bezbradica, Dejan; Kolarski, Dušan; Veličković, Dušan

(Elsevier Sci Ltd, Oxford, 2017)

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Milosavić, Nenad
AU  - Dimitrijević, Aleksandra
AU  - Gavrović-Jankulović, Marija
AU  - Bezbradica, Dejan
AU  - Kolarski, Dušan
AU  - Veličković, Dušan
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2338
AB  - A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases
VL  - 218
SP  - 505
EP  - 508
DO  - 10.1016/j.foodchem.2016.09.049
ER  - 
@article{
author = "Trbojević-Ivić, Jovana and Milosavić, Nenad and Dimitrijević, Aleksandra and Gavrović-Jankulović, Marija and Bezbradica, Dejan and Kolarski, Dušan and Veličković, Dušan",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2338",
abstract = "A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases",
volume = "218",
pages = "505-508",
doi = "10.1016/j.foodchem.2016.09.049"
}
Trbojević-Ivić, J., Milosavić, N., Dimitrijević, A., Gavrović-Jankulović, M., Bezbradica, D., Kolarski, D.,& Veličković, D. (2017). Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases.
Food ChemistryElsevier Sci Ltd, Oxford., 218, 505-508.
https://doi.org/10.1016/j.foodchem.2016.09.049
Trbojević-Ivić J, Milosavić N, Dimitrijević A, Gavrović-Jankulović M, Bezbradica D, Kolarski D, Veličković D. Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases. Food Chemistry. 2017;218:505-508
Trbojević-Ivić Jovana, Milosavić Nenad, Dimitrijević Aleksandra, Gavrović-Jankulović Marija, Bezbradica Dejan, Kolarski Dušan, Veličković Dušan, "Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases" 218 (2017):505-508,
https://doi.org/10.1016/j.foodchem.2016.09.049 .
12
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Macroporous poly(GMA-co-EGDMA) for enzyme stabilization

Milosavić, N.B.; Prodanović, Radivoje; Velićković, D.; Dimitrijević, Aleksandra

(Springer Science+Business Media New York, 2017)

TY  - CHAP
AU  - Milosavić, N.B.
AU  - Prodanović, Radivoje
AU  - Velićković, D.
AU  - Dimitrijević, Aleksandra
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/301
AB  - One of the most used procedures for enzyme stabilization is immobilization. Although immobilization on solid supports has been pursued since the 1950s, there are no general rules for selecting the best support for a giving application. A macroporous copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate (poly (GMA-co-EGDMA)) is a carrier consisting of macroporous beads for immobilizing enzymes of industrial potential for the production of fine chemicals and pharmaceuticals. © Springer Science+Business Media New York 2017.
PB  - Springer Science+Business Media New York
T2  - Methods in Molecular Biology
T1  - Macroporous poly(GMA-co-EGDMA) for enzyme stabilization
VL  - 1504
SP  - 139
EP  - 147
DO  - 10.1007/978-1-4939-6499-4_11
ER  - 
@article{
author = "Milosavić, N.B. and Prodanović, Radivoje and Velićković, D. and Dimitrijević, Aleksandra",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/301",
abstract = "One of the most used procedures for enzyme stabilization is immobilization. Although immobilization on solid supports has been pursued since the 1950s, there are no general rules for selecting the best support for a giving application. A macroporous copolymer of ethylene glycol dimethacrylate and glycidyl methacrylate (poly (GMA-co-EGDMA)) is a carrier consisting of macroporous beads for immobilizing enzymes of industrial potential for the production of fine chemicals and pharmaceuticals. © Springer Science+Business Media New York 2017.",
publisher = "Springer Science+Business Media New York",
journal = "Methods in Molecular Biology",
title = "Macroporous poly(GMA-co-EGDMA) for enzyme stabilization",
volume = "1504",
pages = "139-147",
doi = "10.1007/978-1-4939-6499-4_11"
}
Milosavić, N.B., Prodanović, R., Velićković, D.,& Dimitrijević, A. (2017). Macroporous poly(GMA-co-EGDMA) for enzyme stabilization.
Methods in Molecular BiologySpringer Science+Business Media New York., 1504, 139-147.
https://doi.org/10.1007/978-1-4939-6499-4_11
Milosavić N, Prodanović R, Velićković D, Dimitrijević A. Macroporous poly(GMA-co-EGDMA) for enzyme stabilization. Methods in Molecular Biology. 2017;1504:139-147
Milosavić N.B., Prodanović Radivoje, Velićković D., Dimitrijević Aleksandra, "Macroporous poly(GMA-co-EGDMA) for enzyme stabilization" 1504 (2017):139-147,
https://doi.org/10.1007/978-1-4939-6499-4_11 .
1
1

Mold/aflatoxin contamination of honey bee collected pollen from different Serbian regions

Kostić, Aleksandar Ž.; Petrović, Tanja S.; Krnjaja, Vesna S.; Nedić, Nebojša M.; Tešić, Živoslav Lj.; Milojković-Opsenica, Dušanka; Barać, Miroljub B.; Stanojević, Slađana P.; Pešić, Mirjana B.

(Taylor & Francis Ltd, Abingdon, 2017)

TY  - JOUR
AU  - Kostić, Aleksandar Ž.
AU  - Petrović, Tanja S.
AU  - Krnjaja, Vesna S.
AU  - Nedić, Nebojša M.
AU  - Tešić, Živoslav Lj.
AU  - Milojković-Opsenica, Dušanka
AU  - Barać, Miroljub B.
AU  - Stanojević, Slađana P.
AU  - Pešić, Mirjana B.
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2402
AB  - Assessment of microbiological quality of bee collected pollen is very important, because of its use as a supplement in the human diet. In this study, 26 samples collected from different location in Serbia were tested for the presence of mold through mycologial analysis. The presence of aflatoxin B1, one of the most dangerous and the most widespread mycotoxin was also determined. It was established that 10 of the investigated samples were contaminated with some genera or species of mold, but all of the investigated samples were contaminated with aflatoxin B1. Considering that there is no unique and official procedure for mycological analysis of bee collected pollen, these findings suggest the need for their establishment. Mycological analysis should be followed by mycotoxicological analysis since the absence of mold does not confirm the absence of aflatoxin B1 in bee pollen.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Journal of Apicultural Research
T1  - Mold/aflatoxin contamination of honey bee collected pollen from different Serbian regions
VL  - 56
IS  - 1
SP  - 13
EP  - 20
DO  - 10.1080/00218839.2016.1259897
ER  - 
@article{
author = "Kostić, Aleksandar Ž. and Petrović, Tanja S. and Krnjaja, Vesna S. and Nedić, Nebojša M. and Tešić, Živoslav Lj. and Milojković-Opsenica, Dušanka and Barać, Miroljub B. and Stanojević, Slađana P. and Pešić, Mirjana B.",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2402",
abstract = "Assessment of microbiological quality of bee collected pollen is very important, because of its use as a supplement in the human diet. In this study, 26 samples collected from different location in Serbia were tested for the presence of mold through mycologial analysis. The presence of aflatoxin B1, one of the most dangerous and the most widespread mycotoxin was also determined. It was established that 10 of the investigated samples were contaminated with some genera or species of mold, but all of the investigated samples were contaminated with aflatoxin B1. Considering that there is no unique and official procedure for mycological analysis of bee collected pollen, these findings suggest the need for their establishment. Mycological analysis should be followed by mycotoxicological analysis since the absence of mold does not confirm the absence of aflatoxin B1 in bee pollen.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Journal of Apicultural Research",
title = "Mold/aflatoxin contamination of honey bee collected pollen from different Serbian regions",
volume = "56",
number = "1",
pages = "13-20",
doi = "10.1080/00218839.2016.1259897"
}
Kostić, A. Ž., Petrović, T. S., Krnjaja, V. S., Nedić, N. M., Tešić, Ž. Lj., Milojković-Opsenica, D., Barać, M. B., Stanojević, S. P.,& Pešić, M. B. (2017). Mold/aflatoxin contamination of honey bee collected pollen from different Serbian regions.
Journal of Apicultural ResearchTaylor & Francis Ltd, Abingdon., 56(1), 13-20.
https://doi.org/10.1080/00218839.2016.1259897
Kostić AŽ, Petrović TS, Krnjaja VS, Nedić NM, Tešić ŽL, Milojković-Opsenica D, Barać MB, Stanojević SP, Pešić MB. Mold/aflatoxin contamination of honey bee collected pollen from different Serbian regions. Journal of Apicultural Research. 2017;56(1):13-20
Kostić Aleksandar Ž., Petrović Tanja S., Krnjaja Vesna S., Nedić Nebojša M., Tešić Živoslav Lj., Milojković-Opsenica Dušanka, Barać Miroljub B., Stanojević Slađana P., Pešić Mirjana B., "Mold/aflatoxin contamination of honey bee collected pollen from different Serbian regions" 56, no. 1 (2017):13-20,
https://doi.org/10.1080/00218839.2016.1259897 .
2
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9
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Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports

Mihailović, Mladen; Trbojević-Ivić, Jovana; Banjanac, Katarina; Milosavić, Nenad; Veličković, Dušan; Carević, Milica; Bezbradica, Dejan

(Serbian Chemical Soc, Belgrade, 2016)

TY  - JOUR
AU  - Mihailović, Mladen
AU  - Trbojević-Ivić, Jovana
AU  - Banjanac, Katarina
AU  - Milosavić, Nenad
AU  - Veličković, Dušan
AU  - Carević, Milica
AU  - Bezbradica, Dejan
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2391
AB  - In this study, two commercial supports (Eupergit (R) C and Purolite (R) A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with the cysteine residues on the surface of enzymes. Thereafter, the maltase from Saccharomyces cerevisiae was immobilized onto the obtained thiosulfonate-activated supports, resulting in high expressed enzymatic activities (around 50 %), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5 %. Moreover, protein loadings up to 12.3 mg g(-1) and immobilized activities up to 3580 IU g(-1) were achieved by employment of these thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on the thiosulfonate supports was the first step of fast adsorption onto the supports and the formation of covalent bonds between the thiosulfonate groups and the thiol groups of cysteine represented a second slower step. More importantly, although enzyme coupling occurred via covalent bond formation, the performed immobilization proved to be reversible, since it was shown that 95 % of the immobilized activity could be detached from the support after treatment with a thiol reagent (beta-mercaptoethanol). Thus, the support could be reused after enzyme inactivation.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports
VL  - 81
IS  - 12
SP  - 1371
EP  - 1382
DO  - 10.2298/JSC160730099M
ER  - 
@article{
author = "Mihailović, Mladen and Trbojević-Ivić, Jovana and Banjanac, Katarina and Milosavić, Nenad and Veličković, Dušan and Carević, Milica and Bezbradica, Dejan",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2391",
abstract = "In this study, two commercial supports (Eupergit (R) C and Purolite (R) A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with the cysteine residues on the surface of enzymes. Thereafter, the maltase from Saccharomyces cerevisiae was immobilized onto the obtained thiosulfonate-activated supports, resulting in high expressed enzymatic activities (around 50 %), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5 %. Moreover, protein loadings up to 12.3 mg g(-1) and immobilized activities up to 3580 IU g(-1) were achieved by employment of these thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on the thiosulfonate supports was the first step of fast adsorption onto the supports and the formation of covalent bonds between the thiosulfonate groups and the thiol groups of cysteine represented a second slower step. More importantly, although enzyme coupling occurred via covalent bond formation, the performed immobilization proved to be reversible, since it was shown that 95 % of the immobilized activity could be detached from the support after treatment with a thiol reagent (beta-mercaptoethanol). Thus, the support could be reused after enzyme inactivation.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports",
volume = "81",
number = "12",
pages = "1371-1382",
doi = "10.2298/JSC160730099M"
}
Mihailović, M., Trbojević-Ivić, J., Banjanac, K., Milosavić, N., Veličković, D., Carević, M.,& Bezbradica, D. (2016). Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports.
Journal of the Serbian Chemical SocietySerbian Chemical Soc, Belgrade., 81(12), 1371-1382.
https://doi.org/10.2298/JSC160730099M
Mihailović M, Trbojević-Ivić J, Banjanac K, Milosavić N, Veličković D, Carević M, Bezbradica D. Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports. Journal of the Serbian Chemical Society. 2016;81(12):1371-1382
Mihailović Mladen, Trbojević-Ivić Jovana, Banjanac Katarina, Milosavić Nenad, Veličković Dušan, Carević Milica, Bezbradica Dejan, "Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports" 81, no. 12 (2016):1371-1382,
https://doi.org/10.2298/JSC160730099M .

Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry

Trbojević-Ivić, Jovana; Veličković, Dušan; Dimitrijević, Aleksandra; Bezbradica, Dejan; Dragacevic, Vladimir; Gavrović-Jankulović, Marija; Milosavić, Nenad

(Wiley-Blackwell, Hoboken, 2016)

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bezbradica, Dejan
AU  - Dragacevic, Vladimir
AU  - Gavrović-Jankulović, Marija
AU  - Milosavić, Nenad
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1943
AB  - BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market. (c) 2016 Society of Chemical Industry
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry
VL  - 96
IS  - 12
SP  - 4281
EP  - 4287
DO  - 10.1002/jsfa.7641
ER  - 
@article{
author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Bezbradica, Dejan and Dragacevic, Vladimir and Gavrović-Jankulović, Marija and Milosavić, Nenad",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1943",
abstract = "BACKGROUNDBiocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation. This study presents an easy and time-saving method for immobilizing this valuable enzyme on hydroxyapatite (HAP), a biomaterial with high protein-binding capacity. RESULTSTargeted immobilized CRL was obtained in high yield of 98%. Significant lipase stabilization was observed upon immobilization: at 60 degrees C, immobilized lipase (HAP-CRL) retained almost unchanged activity after 3h, while free CRL lost 50% of its initial activity after only 30min. The same trend was observed with tested organic solvents. Methanol and hexane had the most pronounced effect: after 3h, only HAP-CRL was stable and active, while CRL was completely inactivated. The practical value of the prepared catalyst was tested in the synthesis of the aroma ester methyl acetate in hexane. Reaction yields were 2.6 and 52.5% for CRL and HAP-CRL respectively. CONCLUSIONThis research has successfully combined an industrially prominent biocatalyst, CRL, and a biocompatible, environmentally suitable carrier, HAP, into an immobilized preparation with improved catalytic properties. The obtained CRL preparation has excellent potential for the food and flavor industries, major consumers in the global enzyme market. (c) 2016 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry",
volume = "96",
number = "12",
pages = "4281-4287",
doi = "10.1002/jsfa.7641"
}
Trbojević-Ivić, J., Veličković, D., Dimitrijević, A., Bezbradica, D., Dragacevic, V., Gavrović-Jankulović, M.,& Milosavić, N. (2016). Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry.
Journal of the Science of Food and AgricultureWiley-Blackwell, Hoboken., 96(12), 4281-4287.
https://doi.org/10.1002/jsfa.7641
Trbojević-Ivić J, Veličković D, Dimitrijević A, Bezbradica D, Dragacevic V, Gavrović-Jankulović M, Milosavić N. Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry. Journal of the Science of Food and Agriculture. 2016;96(12):4281-4287
Trbojević-Ivić Jovana, Veličković Dušan, Dimitrijević Aleksandra, Bezbradica Dejan, Dragacevic Vladimir, Gavrović-Jankulović Marija, Milosavić Nenad, "Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry" 96, no. 12 (2016):4281-4287,
https://doi.org/10.1002/jsfa.7641 .
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