Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance

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Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (en)
Алергени, антитела, ензими и мали физиолошки значајни молекули: дизајн, структура, функција и значај (sr)
Alergeni, antitela, enzimi i mali fiziološki značajni molekuli: dizajn, struktura, funkcija i značaj (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

Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors

Vrhovac, Lidija; Šelemetjev, Sonja A.; Vatić, Saša; Mitrović, Aleksandar; Milošević, Jelica; Lolić, Aleksandar; Beletić, Anđelo D.; Polović, Natalija

(Elsevier, 2021)

TY  - JOUR
AU  - Vrhovac, Lidija
AU  - Šelemetjev, Sonja A.
AU  - Vatić, Saša
AU  - Mitrović, Aleksandar
AU  - Milošević, Jelica
AU  - Lolić, Aleksandar
AU  - Beletić, Anđelo D.
AU  - Polović, Natalija
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4295
AB  - Measurement of antithyroglobulin antibodies (TgAb) is an inevitable laboratory tool in the management of thyroid gland diseases. Currently available immunoassays still have limitations underlying the necessity of the introduction of fast, sensitive, and label-free technologies. Our aim was to develop a method for TgAb measurement in human serum based on the quartz crystal microbalance (QCM) technology. We immobilized thyroglobulin on the surface of Attana LNB Carboxyl sensor chip®, prepared standard curve covering the range of 1–50000 kIU/L, and established optimal measurement conditions. The validation included determination of the detection limit (LOD), functional sensitivity, linearity, precision, as well as the comparison with the results of the radioimmunoassay (RIA). The LOD and functional sensitivity were 4.2 kIU/L and 4.7 kIU/L, respectively. The method was linear in the range of 20–10000 kIU/L. The regression equation for comparison with RIA was CQCM = 1.0056 • CRIA – 24.2778, whereby no significant proportional or systematic difference was present. There was a good agreement with RIA in the classification of patients according to the clinical significance of the results. The developed method has advantages over currently available assays in terms of better LOQ, a higher upper limit of linearity, and precision. The characteristics of the developed method unambiguously show that the application of the QCM biosensors offers a highly reliable novel approach for the measurement of TgAb in human serum.
PB  - Elsevier
T2  - Talanta
T1  - Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors
VL  - 223
SP  - 121588
DO  - 10.1016/j.talanta.2020.121588
ER  - 
@article{
author = "Vrhovac, Lidija and Šelemetjev, Sonja A. and Vatić, Saša and Mitrović, Aleksandar and Milošević, Jelica and Lolić, Aleksandar and Beletić, Anđelo D. and Polović, Natalija",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4295",
abstract = "Measurement of antithyroglobulin antibodies (TgAb) is an inevitable laboratory tool in the management of thyroid gland diseases. Currently available immunoassays still have limitations underlying the necessity of the introduction of fast, sensitive, and label-free technologies. Our aim was to develop a method for TgAb measurement in human serum based on the quartz crystal microbalance (QCM) technology. We immobilized thyroglobulin on the surface of Attana LNB Carboxyl sensor chip®, prepared standard curve covering the range of 1–50000 kIU/L, and established optimal measurement conditions. The validation included determination of the detection limit (LOD), functional sensitivity, linearity, precision, as well as the comparison with the results of the radioimmunoassay (RIA). The LOD and functional sensitivity were 4.2 kIU/L and 4.7 kIU/L, respectively. The method was linear in the range of 20–10000 kIU/L. The regression equation for comparison with RIA was CQCM = 1.0056 • CRIA – 24.2778, whereby no significant proportional or systematic difference was present. There was a good agreement with RIA in the classification of patients according to the clinical significance of the results. The developed method has advantages over currently available assays in terms of better LOQ, a higher upper limit of linearity, and precision. The characteristics of the developed method unambiguously show that the application of the QCM biosensors offers a highly reliable novel approach for the measurement of TgAb in human serum.",
publisher = "Elsevier",
journal = "Talanta",
title = "Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors",
volume = "223",
pages = "121588",
doi = "10.1016/j.talanta.2020.121588"
}
Vrhovac, L., Šelemetjev, S. A., Vatić, S., Mitrović, A., Milošević, J., Lolić, A., Beletić, A. D.,& Polović, N. (2021). Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors.
TalantaElsevier., 223, 121588.
https://doi.org/10.1016/j.talanta.2020.121588
Vrhovac L, Šelemetjev SA, Vatić S, Mitrović A, Milošević J, Lolić A, Beletić AD, Polović N. Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors. Talanta. 2021;223:121588
Vrhovac Lidija, Šelemetjev Sonja A., Vatić Saša, Mitrović Aleksandar, Milošević Jelica, Lolić Aleksandar, Beletić Anđelo D., Polović Natalija, "Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors" 223 (2021):121588,
https://doi.org/10.1016/j.talanta.2020.121588 .

Proteinski inženjering ligninolitičkih peroksidaza u cilju unapređenja degradacije tekstilnih boja

Ilić Đurđić, Karla

(Универзитет у Београду, Хемијски факултет, 2020-12-03)

TY  - BOOK
AU  - Ilić Đurđić, Karla
PY  - 2020-12-03
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7851
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:23142/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=30770697
UR  - https://nardus.mpn.gov.rs/handle/123456789/17770
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4363
AB  - Tekstilna industrija iskoristi preko petsto hiljada tona boja godišnje. Neefikasnost procesa bojenja dovodi do otpuštanja izuzetno velikih količina tekstilnih boja u životnu sredinu. Kako je veliki broj studija pokazao da su sintetičke boje, a prevashodno azo boje izuzetno toksične i da predstavljaju pretnju za javno zdravlje njihovo uklanjanje iz životne sredine i otpadnih voda je od velikog značaja. Međutim, kako su sintetičke boje vrlo heterogeni molekuli koji u svojoj strukturi sadrže više funkcionalnih grupa veoma mali broj enzima ima mogućnost da katalizuje degradaciju širokog spektra ovih jedinjenja.
AB  - Textile industry spends over five hundred tons of dyes each year. Inefficiency of dying process releases high amounts of textile dyes to environment. As many synthetic dyes, especially azo dyes are proven to be toxic and represent a risk for public health, their removal from ecosystems and wastewaters is of great importance. However, synthetic dyes are very heterogeneous group of molecules with many different functional groups. Therefore, very few enzymes are able to catalyze their degradation.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Proteinski inženjering ligninolitičkih peroksidaza u cilju unapređenja degradacije tekstilnih boja
ER  - 
@phdthesis{
author = "Ilić Đurđić, Karla",
year = "2020-12-03",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=7851, https://fedorabg.bg.ac.rs/fedora/get/o:23142/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=30770697, https://nardus.mpn.gov.rs/handle/123456789/17770, http://cherry.chem.bg.ac.rs/handle/123456789/4363",
abstract = "Tekstilna industrija iskoristi preko petsto hiljada tona boja godišnje. Neefikasnost procesa bojenja dovodi do otpuštanja izuzetno velikih količina tekstilnih boja u životnu sredinu. Kako je veliki broj studija pokazao da su sintetičke boje, a prevashodno azo boje izuzetno toksične i da predstavljaju pretnju za javno zdravlje njihovo uklanjanje iz životne sredine i otpadnih voda je od velikog značaja. Međutim, kako su sintetičke boje vrlo heterogeni molekuli koji u svojoj strukturi sadrže više funkcionalnih grupa veoma mali broj enzima ima mogućnost da katalizuje degradaciju širokog spektra ovih jedinjenja., Textile industry spends over five hundred tons of dyes each year. Inefficiency of dying process releases high amounts of textile dyes to environment. As many synthetic dyes, especially azo dyes are proven to be toxic and represent a risk for public health, their removal from ecosystems and wastewaters is of great importance. However, synthetic dyes are very heterogeneous group of molecules with many different functional groups. Therefore, very few enzymes are able to catalyze their degradation.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Proteinski inženjering ligninolitičkih peroksidaza u cilju unapređenja degradacije tekstilnih boja"
}
Ilić Đurđić, K. (2020-12-03). Proteinski inženjering ligninolitičkih peroksidaza u cilju unapređenja degradacije tekstilnih boja.
Универзитет у БеоградуУниверзитет у Београду, Хемијски факултет..
Ilić Đurđić K. Proteinski inženjering ligninolitičkih peroksidaza u cilju unapređenja degradacije tekstilnih boja. Универзитет у Београду. 2020;
Ilić Đurđić Karla, "Proteinski inženjering ligninolitičkih peroksidaza u cilju unapređenja degradacije tekstilnih boja" (2020-12-03)

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 .

Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation

Milošević, Jelica; Petrić, Jovan; Jovčić, Branko; Janković, Brankica; Polović, Natalija

(Elsevier, 2020)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3884
AB  - Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation
VL  - 229
DO  - 10.1016/j.saa.2019.117882
ER  - 
@article{
author = "Milošević, Jelica and Petrić, Jovan and Jovčić, Branko and Janković, Brankica and Polović, Natalija",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3884",
abstract = "Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation",
volume = "229",
doi = "10.1016/j.saa.2019.117882"
}
Milošević, J., Petrić, J., Jovčić, B., Janković, B.,& Polović, N. (2020). Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation.
Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyElsevier., 229.
https://doi.org/10.1016/j.saa.2019.117882
Milošević J, Petrić J, Jovčić B, Janković B, Polović N. Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;229
Milošević Jelica, Petrić Jovan, Jovčić Branko, Janković Brankica, Polović Natalija, "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation" 229 (2020),
https://doi.org/10.1016/j.saa.2019.117882 .
3
3
2

Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882

Milošević, Jelica; Petrić, Jovan; Jovčić, Branko; Janković, Brankica; Polović, Natalija

(Elsevier, 2020)

TY  - BOOK
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3894
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882
ER  - 
@book{
author = "Milošević, Jelica and Petrić, Jovan and Jovčić, Branko and Janković, Brankica and Polović, Natalija",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3894",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882"
}
Milošević, J., Petrić, J., Jovčić, B., Janković, B.,& Polović, N. (2020). Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882.
Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyElsevier..
Milošević J, Petrić J, Jovčić B, Janković B, Polović N. Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;
Milošević Jelica, Petrić Jovan, Jovčić Branko, Janković Brankica, Polović Natalija, "Supplementary data for the article: Milošević, J.; Petrić, J.; Jovčić, B.; Janković, B.; Polović, N. Exploring the Potential of Infrared Spectroscopy in Qualitative and Quantitative Monitoring of Ovalbumin Amyloid Fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 2020, 229. https://doi.org/10.1016/j.saa.2019.117882" (2020)

Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation

Milošević, Jelica; Petrić, Jovan; Jovčić, Branko; Janković, Brankica; Polović, Natalija

(Elsevier, 2020)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Petrić, Jovan
AU  - Jovčić, Branko
AU  - Janković, Brankica
AU  - Polović, Natalija
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3895
AB  - Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.
PB  - Elsevier
T2  - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
T1  - Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation
VL  - 229
DO  - 10.1016/j.saa.2019.117882
ER  - 
@article{
author = "Milošević, Jelica and Petrić, Jovan and Jovčić, Branko and Janković, Brankica and Polović, Natalija",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3895",
abstract = "Amyloid fibrils are highly ordered self-assembled (poly)peptide aggregates with cross-β structural pattern. Ovalbumin was used as a model for exploring the potential of infrared spectroscopy in detecting structural transitions and quantitative monitoring of amyloid fibrillation. Low pH (pH 2) and high temperature (90 °C) over the course of 24 h were conditions applied for amyloid formation. Fibrillation of ovalbumin was monitored by ThT and ANS fluorescence, and SDS PAGE. A significant increase in ThT fluorescence with a plateau reached after 4 h of incubation, without the lag phase, was detected. Structural transitions leading to amyloid fibrillation were analysed using all three Amide regions in ATR-FTIR spectra. Significant changes were detected in Amide I and Amide III region (decrease of α-helix and increase of β-sheet peaks). To establish a fast, precise and simple method for quantitative monitoring of amyloid fibrillation, the Amide I/Amide II ratios of aggregation specific β-sheets (1625 and 1695 cm−1, respectively) with 1540 cm−1 as internal standard were used, resulting in good correlation (R2 = 0.93 and 0.95) with the data observed by monitoring ThT fluorescence. On the other hand, assessing aggregation specific β-sheet contents by self-deconvolution showed lower correlation with ThT fluorescence (R2 = 0.75 and 0.64). Here we examined structural transitions during ovalbumin fibrillation in a qualitative and quantitative manner by exploiting the full potential of Amide regions simultaneously. Secondary structure distribution was monitored using second derivative spectra in Amide I region. A novel, simple mathematical calculation for quantitative monitoring of fibrils formation was presented employing that the increase in low and high frequency aggregation specific β-sheet in Amide I region compared to the internal standard in Amide II region is suitable for fibril formation monitoring.",
publisher = "Elsevier",
journal = "Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy",
title = "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation",
volume = "229",
doi = "10.1016/j.saa.2019.117882"
}
Milošević, J., Petrić, J., Jovčić, B., Janković, B.,& Polović, N. (2020). Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation.
Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyElsevier., 229.
https://doi.org/10.1016/j.saa.2019.117882
Milošević J, Petrić J, Jovčić B, Janković B, Polović N. Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. 2020;229
Milošević Jelica, Petrić Jovan, Jovčić Branko, Janković Brankica, Polović Natalija, "Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation" 229 (2020),
https://doi.org/10.1016/j.saa.2019.117882 .
3
3
2

Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa

Minić, Rajna; Josipović, Mirjana; Tomić Spirić, Vesna; Gavrović-Jankulović, Marija; Perić Popadić, Aleksandra; Prokopijević, Ivana; Ljubičić, Ana; Stamenković, Danijela; Burazer, Lidija M.

(MDPI, 2020)

TY  - JOUR
AU  - Minić, Rajna
AU  - Josipović, Mirjana
AU  - Tomić Spirić, Vesna
AU  - Gavrović-Jankulović, Marija
AU  - Perić Popadić, Aleksandra
AU  - Prokopijević, Ivana
AU  - Ljubičić, Ana
AU  - Stamenković, Danijela
AU  - Burazer, Lidija M.
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3883
AB  - Background and objectives: The relationship between air pollen quantity and the sensitization of allergic patients is crucial for both the diagnosis and treatment of allergic diseases. Weather conditions influence the distribution of allergenic pollen and increases in pollen concentration may negatively affect the health of allergic patients. The aim of this study was to analyze the implementation of allergen immunotherapy with regard to air pollen concentration. Material and Methods: Here we examined the relationship between Betula air pollen concentration and the usage of Betula verrucosa allergen immunotherapy in Serbia. Examination covered the period from 2015 to 2018. Measurement of airborne pollen concentration was performed with Lanzoni volumetric pollen traps. The evidence of the usage of sublingual allergen immunotherapy (SLIT) was gathered from patients with documented sensitization to specific pollen. Results: During this period tree pollens were represented with 58% ± 21% of all measured air pollen species, while Betula pollen represented 15% ± 8% of all tree pollens. Betula pollination peaked in April. Allergen immunotherapy to Betula verrucosa in Serbia is entirely conducted as sublingual immunotherapy and represents 47.1% ± 1.4% of issued tree pollen SLIT. The use of pollen SLIT increased by 68% from 2015 to 2018, with an even greater increase in usage recorded for Betula SLIT—80%. Conclusions: This analysis shows a clear causative relationship between pollination and the type/prevalence of applied allergen immunotherapy. Information about the flowering seasons of allergenic plants is very important for people who suffer from allergy, for clinical allergologists, as well as for governing authorities. The presented data is of practical importance to the proper timing of immunotherapy initiation and of importance for urban landscaping. The obtained data can be the starting point for the instatement of a thorough epidemiological study and the inclusion of Serbia on the pollen map of Europe.
PB  - MDPI
T2  - Medicina (Lithuania)
T1  - Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa
VL  - 56
IS  - 2
DO  - 10.3390/medicina56020059
ER  - 
@article{
author = "Minić, Rajna and Josipović, Mirjana and Tomić Spirić, Vesna and Gavrović-Jankulović, Marija and Perić Popadić, Aleksandra and Prokopijević, Ivana and Ljubičić, Ana and Stamenković, Danijela and Burazer, Lidija M.",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3883",
abstract = "Background and objectives: The relationship between air pollen quantity and the sensitization of allergic patients is crucial for both the diagnosis and treatment of allergic diseases. Weather conditions influence the distribution of allergenic pollen and increases in pollen concentration may negatively affect the health of allergic patients. The aim of this study was to analyze the implementation of allergen immunotherapy with regard to air pollen concentration. Material and Methods: Here we examined the relationship between Betula air pollen concentration and the usage of Betula verrucosa allergen immunotherapy in Serbia. Examination covered the period from 2015 to 2018. Measurement of airborne pollen concentration was performed with Lanzoni volumetric pollen traps. The evidence of the usage of sublingual allergen immunotherapy (SLIT) was gathered from patients with documented sensitization to specific pollen. Results: During this period tree pollens were represented with 58% ± 21% of all measured air pollen species, while Betula pollen represented 15% ± 8% of all tree pollens. Betula pollination peaked in April. Allergen immunotherapy to Betula verrucosa in Serbia is entirely conducted as sublingual immunotherapy and represents 47.1% ± 1.4% of issued tree pollen SLIT. The use of pollen SLIT increased by 68% from 2015 to 2018, with an even greater increase in usage recorded for Betula SLIT—80%. Conclusions: This analysis shows a clear causative relationship between pollination and the type/prevalence of applied allergen immunotherapy. Information about the flowering seasons of allergenic plants is very important for people who suffer from allergy, for clinical allergologists, as well as for governing authorities. The presented data is of practical importance to the proper timing of immunotherapy initiation and of importance for urban landscaping. The obtained data can be the starting point for the instatement of a thorough epidemiological study and the inclusion of Serbia on the pollen map of Europe.",
publisher = "MDPI",
journal = "Medicina (Lithuania)",
title = "Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa",
volume = "56",
number = "2",
doi = "10.3390/medicina56020059"
}
Minić, R., Josipović, M., Tomić Spirić, V., Gavrović-Jankulović, M., Perić Popadić, A., Prokopijević, I., Ljubičić, A., Stamenković, D.,& Burazer, L. M. (2020). Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa.
Medicina (Lithuania)MDPI., 56(2).
https://doi.org/10.3390/medicina56020059
Minić R, Josipović M, Tomić Spirić V, Gavrović-Jankulović M, Perić Popadić A, Prokopijević I, Ljubičić A, Stamenković D, Burazer LM. Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa. Medicina (Lithuania). 2020;56(2)
Minić Rajna, Josipović Mirjana, Tomić Spirić Vesna, Gavrović-Jankulović Marija, Perić Popadić Aleksandra, Prokopijević Ivana, Ljubičić Ana, Stamenković Danijela, Burazer Lidija M., "Impact of tree pollen distribution on allergic diseases in serbia: Evidence of implementation of allergen immunotherapy to Betula verrucosa" 56, no. 2 (2020),
https://doi.org/10.3390/medicina56020059 .
1
1
1
1

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

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

(Applied sciences, 2019)

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

Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation

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

(The Polymer Society of Korea, 2019)

TY  - JOUR
AU  - Spasojević, Dragica
AU  - Prokopijević, Miloš
AU  - Prodanović, Olivera
AU  - Zelenović, Nevena D.
AU  - Polović, Natalija
AU  - Radotić, Ksenija
AU  - Prodanović, Radivoje
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3732
AB  - Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.
PB  - The Polymer Society of Korea
T2  - Macromolecular Research
T1  - Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation
VL  - 27
IS  - 8
SP  - 764
EP  - 771
DO  - 10.1007/s13233-019-7111-7
ER  - 
@article{
author = "Spasojević, Dragica and Prokopijević, Miloš and Prodanović, Olivera and Zelenović, Nevena D. and Polović, Natalija and Radotić, Ksenija and Prodanović, Radivoje",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3732",
abstract = "Derivatives of xylans were synthesized from corncob xylan by carboxymethylation, oxidization with different molar ratios of periodate (5, 10 15 and 20 mol%) and by reductive amination with tyramine. Modifications of tyramine carboxymethyl xylans (Tyr-CMX) were confirmed by FTIR, UV and NMR spectra. Concentration of ionizable groups increased from 1.5 mmol/g for carboxymethyl xylan (CMX) to 5.4 mmol/g for Tyr-CMX oxidized with 20 mol% of periodate. All Tyr-CMXs were able to form hydrogels the cross-linking reaction with horseradish peroxidase and peroxide. Tyr-CMXs were tested for amyloglucosidase (AG) encapsulation within hydrogel microbeads obtained in a reaction of emulsion polymerization with peroxidase. Average diameter of Tyr-CMX hydrogel microbeads was 52±25 µm and after encapsulation optimization with respect to the extent of CMX modification with tyramine, the concentration of Tyr-CMX, and the amount of added AG, microbeads with AG specific activity of 2 U/mL and 20% yield of immobilization were obtained. The optimum pH of the immobilized AG was not changed compared to the soluble one, while half-life at 60 °C was increased around 10 times. The Michaelis-Menten constant for the immobilized enzyme, 1.03 mM, was significantly lower than that for the soluble one, 1.54 mM. After 5 cycles of repetitive use in batch reactor, the immobilized AG retained 68% of initial activity.",
publisher = "The Polymer Society of Korea",
journal = "Macromolecular Research",
title = "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation",
volume = "27",
number = "8",
pages = "764-771",
doi = "10.1007/s13233-019-7111-7"
}
Spasojević, D., Prokopijević, M., Prodanović, O., Zelenović, N. D., Polović, N., Radotić, K.,& Prodanović, R. (2019). Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation.
Macromolecular ResearchThe Polymer Society of Korea., 27(8), 764-771.
https://doi.org/10.1007/s13233-019-7111-7
Spasojević D, Prokopijević M, Prodanović O, Zelenović ND, Polović N, Radotić K, Prodanović R. Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation. Macromolecular Research. 2019;27(8):764-771
Spasojević Dragica, Prokopijević Miloš, Prodanović Olivera, Zelenović Nevena D., Polović Natalija, Radotić Ksenija, Prodanović Radivoje, "Peroxidase-Sensitive Tyramine Carboxymethyl Xylan Hydrogels for Enzyme Encapsulation" 27, no. 8 (2019):764-771,
https://doi.org/10.1007/s13233-019-7111-7 .
1
2
2

Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj

Trbojević Ivić, Jovana

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - BOOK
AU  - Trbojević Ivić, Jovana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7117
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:20779/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=51817999
UR  - http://nardus.mpn.gov.rs/123456789/11808
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3911
AB  - U ovoj doktorskoj disertaciji je ispitan potencijal HAP za imobilizaciju industrijski značajnih enzima na primeru 4 lipaze i 4 glikozidaze različitog porekla, strukture i supstratne specifičnosti. Od testiranih enzima za HAP se najefikasnije vezuju lipaza iz Candida rugosa (CRL) i β-galaktozidaza (laktaza) iz Aspergillus oryzae (AOL). Oba enzima se imobilizuju na HAP jednostavnom, brzom i efikasnom fizičkom adsorpcijom po mehanizmu metal-koordinatne veze. Kombinovanjem bioinformatičkog pristupa i molekulskog modelovanja za oba enzima su identifikovani i opisani površinski HAP-vezujući motivi.Imobilizacija na HAP je uzrokovala promenu supstratne specifičnosti CRL ka supstratima sa kraćim alkil-nizom i drastično povećanje stabilnosti i aktivnosti enzima u metanolu. Ove karakteristike imobilizata CRL na HAP (CRL-HAP) su prvi put u literaturi primenjene za sintezu metil-acetata, estra sa mirisom jabuke, koga slobodna CRL sintetiše u zanemarljivom prinosu. Pažljivim odabirom rastvarača i supstrata je, takođe po prvi put pokazano kako ovaj popularni i jeftin enzim, u slobodnom ili imobilizovanom obliku, može da se primeni i za efikasnu sintezu kapsinoida direktnom esterifikacijom vanilil-alkohola (VA) i masnih kiselina (MK) i transesterifikacijom kokosovog ulja.Efikasnost imobilizovanog preparata AOL (AOL-HAP) je ispitana u sintezi bioaktivnih supstanci, vanilil-galaktozida (VG) i galakto-oligosaharida (GOS). Po efikasnosti u sintezi ovih proizvoda preparat AOL-HAP se našao u rangu sa kovalentno imobilizovanim preparatima AOL. Jedna ista šarža AOL-HAP može se iskoristiti u 10 uzastopnih reakcionih ciklusa sinteze VG, odnosno GOS, sa poluživotom od 15 h.
AB  - Potential of hydroxyapatite (HAP) as immobilization carrier for industrially important enzymes was examined in a study, comprising of 4 lipases and 4 glycosidases of different origin, structure and substrate specificity. Lipase from Candida rugosa (CRL) and β-galactosidase (lactase) from Aspergillus oryzae (AOL) exhibited the most efficient binding to HAP. Both of the enzymes were immobilized on HAP by simple, fast and efficient physical adsorption through formation of metal-coordinative bond. Furthermore, by the combining of bioinformatic approach and molecular modeling, HAP-speciffic superficial motif on both selected enzymes was identified and described for the first time in the literature.Immobilization on HAP has shifted substrate specificity of CRL towards shorter alkyl-chains, coupled with significant increase in stability and activity of CRL in methanol. These characteristics of immobilized Candida rugosa lipase preparation (CRL-HAP) were sucessfully implemented in synthesis of methyl-acetate, an apple flavour for the first time in the literature. Free CRL synthesized methyl-acetate in very low yield, because of methanol-induced inactivation. By a meticulous selection of organic solvent and susbtrates, it was shown also for the first time that this popular and cost-effective microbial lipase, free or immobilized on HAP, can be used for efficient synthesis of capsinoids in two distinctive reactions: direct esterification of vanillyl-alcohol (VA) with free fatty acids and transesterification of coconut oil.Efficiency of AOL immobilized on HAP (AOL-HAP), was evaluated in synthesis of bioactive compounds: vanillyl-galactoside (VG) and galacto-oligosaccharide (GOS) probiotics. Efficiency of AOL-HAP in synthesis of these compounds was in a good correlation with the procedures in which covalently immobilized AOL was employed. Immobilized AOL preparation can be used in maximum 10 consecutive reaction cycles during VG and GOS synthesis, with the half-life of 15 hours.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj
ER  - 
@phdthesis{
author = "Trbojević Ivić, Jovana",
year = "2019",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=7117, https://fedorabg.bg.ac.rs/fedora/get/o:20779/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=51817999, http://nardus.mpn.gov.rs/123456789/11808, http://cherry.chem.bg.ac.rs/handle/123456789/3911",
abstract = "U ovoj doktorskoj disertaciji je ispitan potencijal HAP za imobilizaciju industrijski značajnih enzima na primeru 4 lipaze i 4 glikozidaze različitog porekla, strukture i supstratne specifičnosti. Od testiranih enzima za HAP se najefikasnije vezuju lipaza iz Candida rugosa (CRL) i β-galaktozidaza (laktaza) iz Aspergillus oryzae (AOL). Oba enzima se imobilizuju na HAP jednostavnom, brzom i efikasnom fizičkom adsorpcijom po mehanizmu metal-koordinatne veze. Kombinovanjem bioinformatičkog pristupa i molekulskog modelovanja za oba enzima su identifikovani i opisani površinski HAP-vezujući motivi.Imobilizacija na HAP je uzrokovala promenu supstratne specifičnosti CRL ka supstratima sa kraćim alkil-nizom i drastično povećanje stabilnosti i aktivnosti enzima u metanolu. Ove karakteristike imobilizata CRL na HAP (CRL-HAP) su prvi put u literaturi primenjene za sintezu metil-acetata, estra sa mirisom jabuke, koga slobodna CRL sintetiše u zanemarljivom prinosu. Pažljivim odabirom rastvarača i supstrata je, takođe po prvi put pokazano kako ovaj popularni i jeftin enzim, u slobodnom ili imobilizovanom obliku, može da se primeni i za efikasnu sintezu kapsinoida direktnom esterifikacijom vanilil-alkohola (VA) i masnih kiselina (MK) i transesterifikacijom kokosovog ulja.Efikasnost imobilizovanog preparata AOL (AOL-HAP) je ispitana u sintezi bioaktivnih supstanci, vanilil-galaktozida (VG) i galakto-oligosaharida (GOS). Po efikasnosti u sintezi ovih proizvoda preparat AOL-HAP se našao u rangu sa kovalentno imobilizovanim preparatima AOL. Jedna ista šarža AOL-HAP može se iskoristiti u 10 uzastopnih reakcionih ciklusa sinteze VG, odnosno GOS, sa poluživotom od 15 h., Potential of hydroxyapatite (HAP) as immobilization carrier for industrially important enzymes was examined in a study, comprising of 4 lipases and 4 glycosidases of different origin, structure and substrate specificity. Lipase from Candida rugosa (CRL) and β-galactosidase (lactase) from Aspergillus oryzae (AOL) exhibited the most efficient binding to HAP. Both of the enzymes were immobilized on HAP by simple, fast and efficient physical adsorption through formation of metal-coordinative bond. Furthermore, by the combining of bioinformatic approach and molecular modeling, HAP-speciffic superficial motif on both selected enzymes was identified and described for the first time in the literature.Immobilization on HAP has shifted substrate specificity of CRL towards shorter alkyl-chains, coupled with significant increase in stability and activity of CRL in methanol. These characteristics of immobilized Candida rugosa lipase preparation (CRL-HAP) were sucessfully implemented in synthesis of methyl-acetate, an apple flavour for the first time in the literature. Free CRL synthesized methyl-acetate in very low yield, because of methanol-induced inactivation. By a meticulous selection of organic solvent and susbtrates, it was shown also for the first time that this popular and cost-effective microbial lipase, free or immobilized on HAP, can be used for efficient synthesis of capsinoids in two distinctive reactions: direct esterification of vanillyl-alcohol (VA) with free fatty acids and transesterification of coconut oil.Efficiency of AOL immobilized on HAP (AOL-HAP), was evaluated in synthesis of bioactive compounds: vanillyl-galactoside (VG) and galacto-oligosaccharide (GOS) probiotics. Efficiency of AOL-HAP in synthesis of these compounds was in a good correlation with the procedures in which covalently immobilized AOL was employed. Immobilized AOL preparation can be used in maximum 10 consecutive reaction cycles during VG and GOS synthesis, with the half-life of 15 hours.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj"
}
Trbojević Ivić, J. (2019). Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj.
Универзитет у БеоградуУниверзитет у Београду, Хемијски факултет..
Trbojević Ivić J. Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj. Универзитет у Београду. 2019;
Trbojević Ivić Jovana, "Novi aspekti upotrebe hidroksiapatita kao nosača za imobilizaciju industrijski značajnih lipaza i glikozidaza - dizajn, ispitivanje mehanizama vezivanja, stabilnost, primena i značaj" (2019)

Comparative stability of ficin and papain in acidic conditions and the presence of ethanol

Milošević, Jelica; Janković, Brankica; Prodanović, Radivoje; Polović, Natalija

(Springer, 2019)

TY  - JOUR
AU  - Milošević, Jelica
AU  - Janković, Brankica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3932
AB  - Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic-alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic-acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration.
PB  - Springer
T2  - Amino Acids
T1  - Comparative stability of ficin and papain in acidic conditions and the presence of ethanol
VL  - 51
IS  - 5
SP  - 829
EP  - 838
DO  - 10.1007/s00726-019-02724-3
ER  - 
@article{
author = "Milošević, Jelica and Janković, Brankica and Prodanović, Radivoje and Polović, Natalija",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3932",
abstract = "Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic-alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic-acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration.",
publisher = "Springer",
journal = "Amino Acids",
title = "Comparative stability of ficin and papain in acidic conditions and the presence of ethanol",
volume = "51",
number = "5",
pages = "829-838",
doi = "10.1007/s00726-019-02724-3"
}
Milošević, J., Janković, B., Prodanović, R.,& Polović, N. (2019). Comparative stability of ficin and papain in acidic conditions and the presence of ethanol.
Amino AcidsSpringer., 51(5), 829-838.
https://doi.org/10.1007/s00726-019-02724-3
Milošević J, Janković B, Prodanović R, Polović N. Comparative stability of ficin and papain in acidic conditions and the presence of ethanol. Amino Acids. 2019;51(5):829-838
Milošević Jelica, Janković Brankica, Prodanović Radivoje, Polović Natalija, "Comparative stability of ficin and papain in acidic conditions and the presence of ethanol" 51, no. 5 (2019):829-838,
https://doi.org/10.1007/s00726-019-02724-3 .
6
4
7

Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3

Milošević, Jelica; Janković, Brankica; Prodanović, Radivoje; Polović, Natalija

(Springer, 2019)

TY  - BOOK
AU  - Milošević, Jelica
AU  - Janković, Brankica
AU  - Prodanović, Radivoje
AU  - Polović, Natalija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3933
PB  - Springer
T2  - Amino Acids
T1  - Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3
ER  - 
@book{
author = "Milošević, Jelica and Janković, Brankica and Prodanović, Radivoje and Polović, Natalija",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3933",
publisher = "Springer",
journal = "Amino Acids",
title = "Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3"
}
Milošević, J., Janković, B., Prodanović, R.,& Polović, N. (2019). Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3.
Amino AcidsSpringer..
Milošević J, Janković B, Prodanović R, Polović N. Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3. Amino Acids. 2019;
Milošević Jelica, Janković Brankica, Prodanović Radivoje, Polović Natalija, "Supplementary data for the article: Milošević, J.; Janković, B.; Prodanović, R.; Polović, N. Comparative Stability of Ficin and Papain in Acidic Conditions and the Presence of Ethanol. Amino Acids 2019, 51 (5), 829–838. https://doi.org/10.1007/s00726-019-02724-3" (2019)

Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model

Nešić, Andrijana; Stam, Annemarie; Čavić, Milena; Ten Klooster, Jean Paul; Pieters, Raymond; Smit, Joost; Gavrović-Jankulović, Marija

(2019)

TY  - JOUR
AU  - Nešić, Andrijana
AU  - Stam, Annemarie
AU  - Čavić, Milena
AU  - Ten Klooster, Jean Paul
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2019
UR  - https://www.scopus.com/inward/record.uri?eid=2-s2.0-85071845404&doi=10.1016%2fj.jff.2019.103556&partnerID=40&md5=c210fd8346babe18cc93e9b0994c4a1e
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3485
AB  - In this study, two intestinal models were employed to assess the modulatory potential of a major kiwifruit allergen on the innate immunity of epithelial cells. Effects of Act d 1 were analyzed in terms of gene expression and structural changes of tight junction (TJ) proteins, as well as up-regulation of pro-inflammatory cytokines in Caco-2 cells and, for the first time, in mouse-derived intestinal 2-dimensional (2D) organoids.

Biologically active Act d 1 induced up-regulation of TJ genes for CLDN-2, CLDN-3, CLDN-4, ZO-1, and on the protein level induced release of pro-inflammatory cytokines IL-1β, TNFα and IL-33 in both employed model systems. In 2D-organoids, active Act d 1 impaired the TJ protein networks of E-cadherin, claudin-3, and ZO-1.

2D-organoids generated from mouse intestine are a promising new model system for the assessment of allergen-induced intestinal cell responses and a useful tool for mitigation of risks associated with novel food proteins.
T2  - Journal of Functional Foods
T1  - Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model
VL  - 62
DO  - 10.1016/j.jff.2019.103556
ER  - 
@article{
author = "Nešić, Andrijana and Stam, Annemarie and Čavić, Milena and Ten Klooster, Jean Paul and Pieters, Raymond and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2019",
url = "https://www.scopus.com/inward/record.uri?eid=2-s2.0-85071845404&doi=10.1016%2fj.jff.2019.103556&partnerID=40&md5=c210fd8346babe18cc93e9b0994c4a1e, http://cherry.chem.bg.ac.rs/handle/123456789/3485",
abstract = "In this study, two intestinal models were employed to assess the modulatory potential of a major kiwifruit allergen on the innate immunity of epithelial cells. Effects of Act d 1 were analyzed in terms of gene expression and structural changes of tight junction (TJ) proteins, as well as up-regulation of pro-inflammatory cytokines in Caco-2 cells and, for the first time, in mouse-derived intestinal 2-dimensional (2D) organoids.

Biologically active Act d 1 induced up-regulation of TJ genes for CLDN-2, CLDN-3, CLDN-4, ZO-1, and on the protein level induced release of pro-inflammatory cytokines IL-1β, TNFα and IL-33 in both employed model systems. In 2D-organoids, active Act d 1 impaired the TJ protein networks of E-cadherin, claudin-3, and ZO-1.

2D-organoids generated from mouse intestine are a promising new model system for the assessment of allergen-induced intestinal cell responses and a useful tool for mitigation of risks associated with novel food proteins.",
journal = "Journal of Functional Foods",
title = "Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model",
volume = "62",
doi = "10.1016/j.jff.2019.103556"
}
Nešić, A., Stam, A., Čavić, M., Ten Klooster, J. P., Pieters, R., Smit, J.,& Gavrović-Jankulović, M. (2019). Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model.
Journal of Functional Foods, 62.
https://doi.org/10.1016/j.jff.2019.103556
Nešić A, Stam A, Čavić M, Ten Klooster JP, Pieters R, Smit J, Gavrović-Jankulović M. Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model. Journal of Functional Foods. 2019;62
Nešić Andrijana, Stam Annemarie, Čavić Milena, Ten Klooster Jean Paul, Pieters Raymond, Smit Joost, Gavrović-Jankulović Marija, "Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model" 62 (2019),
https://doi.org/10.1016/j.jff.2019.103556 .
1
1
1

Hypersensitivity reactions to antiepileptic drugs in children

Atanasković-Marković, Marina; Janković, Jelena; Tmušić, Vladimir; Gavrović-Jankulović, Marija; Ćirković-Veličković, Tanja; Nikolić, Dimitrije; Škorić, Dejan

(John Wiley and Sons Ltd., 2019)

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Janković, Jelena
AU  - Tmušić, Vladimir
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Nikolić, Dimitrije
AU  - Škorić, Dejan
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3704
AB  - Background: Antiepileptic drugs (AEDs) can cause hypersensitivity reactions in children. These reactions are mainly cutaneous, self-limiting, and benign, but life-threatening severe cutaneous adverse reactions can occur. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions, if a drug is taken at the same time. The aims of our study were to confirm or rule out the diagnosis of hypersensitivity reactions to AEDs in children and to detect an infection which mimics these reactions. Methods: A prospective survey was conducted in a group of 100 children with histories of hypersensitivity reactions to AEDs by performing patch tests, delayed-reading intradermal test, and, in case of negative results, challenge test. In all children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. Results: Maculopapular exanthema and delayed-appearing urticaria were the most reported hypersensitivity reactions to AEDs. Sixty-six (66%) of 100 children had confirmed hypersensitivity reactions to AEDs. Fifty-nine children had positive patch test. No children had positive challenge tests. The most common AEDs causing hypersensitivity reactions were carbamazepine (45.4%) and lamotrigine (43.6%). Thirty-two children had positive tests for viruses or M pneumoniae, and nine of them had also a positive allergy work-up. Conclusion: Considering that there are no specific tests to distinguish between a viral infection and hypersensitivity reactions to AEDs in the acute phase, a diagnostic work-up should be performed in all children with suspected hypersensitivity reactions to AEDs, as well as infectious agent study, to remove a false label of hypersensitivity.
PB  - John Wiley and Sons Ltd.
T2  - Pediatric Allergy and Immunology
T1  - Hypersensitivity reactions to antiepileptic drugs in children
VL  - 30
IS  - 5
SP  - 547
EP  - 552
DO  - 10.1111/pai.13055
ER  - 
@article{
author = "Atanasković-Marković, Marina and Janković, Jelena and Tmušić, Vladimir and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Nikolić, Dimitrije and Škorić, Dejan",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3704",
abstract = "Background: Antiepileptic drugs (AEDs) can cause hypersensitivity reactions in children. These reactions are mainly cutaneous, self-limiting, and benign, but life-threatening severe cutaneous adverse reactions can occur. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions, if a drug is taken at the same time. The aims of our study were to confirm or rule out the diagnosis of hypersensitivity reactions to AEDs in children and to detect an infection which mimics these reactions. Methods: A prospective survey was conducted in a group of 100 children with histories of hypersensitivity reactions to AEDs by performing patch tests, delayed-reading intradermal test, and, in case of negative results, challenge test. In all children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. Results: Maculopapular exanthema and delayed-appearing urticaria were the most reported hypersensitivity reactions to AEDs. Sixty-six (66%) of 100 children had confirmed hypersensitivity reactions to AEDs. Fifty-nine children had positive patch test. No children had positive challenge tests. The most common AEDs causing hypersensitivity reactions were carbamazepine (45.4%) and lamotrigine (43.6%). Thirty-two children had positive tests for viruses or M pneumoniae, and nine of them had also a positive allergy work-up. Conclusion: Considering that there are no specific tests to distinguish between a viral infection and hypersensitivity reactions to AEDs in the acute phase, a diagnostic work-up should be performed in all children with suspected hypersensitivity reactions to AEDs, as well as infectious agent study, to remove a false label of hypersensitivity.",
publisher = "John Wiley and Sons Ltd.",
journal = "Pediatric Allergy and Immunology",
title = "Hypersensitivity reactions to antiepileptic drugs in children",
volume = "30",
number = "5",
pages = "547-552",
doi = "10.1111/pai.13055"
}
Atanasković-Marković, M., Janković, J., Tmušić, V., Gavrović-Jankulović, M., Ćirković-Veličković, T., Nikolić, D.,& Škorić, D. (2019). Hypersensitivity reactions to antiepileptic drugs in children.
Pediatric Allergy and ImmunologyJohn Wiley and Sons Ltd.., 30(5), 547-552.
https://doi.org/10.1111/pai.13055
Atanasković-Marković M, Janković J, Tmušić V, Gavrović-Jankulović M, Ćirković-Veličković T, Nikolić D, Škorić D. Hypersensitivity reactions to antiepileptic drugs in children. Pediatric Allergy and Immunology. 2019;30(5):547-552
Atanasković-Marković Marina, Janković Jelena, Tmušić Vladimir, Gavrović-Jankulović Marija, Ćirković-Veličković Tanja, Nikolić Dimitrije, Škorić Dejan, "Hypersensitivity reactions to antiepileptic drugs in children" 30, no. 5 (2019):547-552,
https://doi.org/10.1111/pai.13055 .
1
6
3
6

Disposable Biosensor Based on Amidase/CeO2/GNR Modified Inkjet-printed CNT Electrodes-droplet Based Paracetamol Detection in Biological Fluids for “Point-of-care” Applications

Stanković, Dalibor; Ognjanović, Miloš; Jović, Milica; Cuplić, Valentina; Lesch, Andreas; Girault, Hubert H.; Gavrović-Jankulović, Marija; Antić, Bratislav

(Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, 2019)

TY  - JOUR
AU  - Stanković, Dalibor
AU  - Ognjanović, Miloš
AU  - Jović, Milica
AU  - Cuplić, Valentina
AU  - Lesch, Andreas
AU  - Girault, Hubert H.
AU  - Gavrović-Jankulović, Marija
AU  - Antić, Bratislav
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3718
AB  - A disposable acetaminophen biosensor based on inkjet-printed CNT electrodes (IJPCNT) modified with amidase/cerium dioxide@graphene nanoribbons composite was developed (ACeO2@GNR/IJPCNT). The enzyme amidase A was used for the first time as a recognition element. Inkjet-printed CNT electrodes served as a basis for the construction of a biosensor that enables droplet detection using 5 μL sample volume. The biosensor showed high selectivity, sensitivity, a low detection limit of 0.18 μM and a wide working linear range from 1 to 100 μM. The proposed approach allows fast and reliable detection of acetaminophen in biological fluids with negligible matrix effect and remarkable reproducibility.
PB  - Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
T2  - Electroanalysis
T1  - Disposable Biosensor Based on Amidase/CeO2/GNR Modified Inkjet-printed CNT Electrodes-droplet Based Paracetamol Detection in Biological Fluids for “Point-of-care” Applications
VL  - 31
IS  - 8
SP  - 1534
EP  - 1542
DO  - 10.1002/elan.201900129
ER  - 
@article{
author = "Stanković, Dalibor and Ognjanović, Miloš and Jović, Milica and Cuplić, Valentina and Lesch, Andreas and Girault, Hubert H. and Gavrović-Jankulović, Marija and Antić, Bratislav",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3718",
abstract = "A disposable acetaminophen biosensor based on inkjet-printed CNT electrodes (IJPCNT) modified with amidase/cerium dioxide@graphene nanoribbons composite was developed (ACeO2@GNR/IJPCNT). The enzyme amidase A was used for the first time as a recognition element. Inkjet-printed CNT electrodes served as a basis for the construction of a biosensor that enables droplet detection using 5 μL sample volume. The biosensor showed high selectivity, sensitivity, a low detection limit of 0.18 μM and a wide working linear range from 1 to 100 μM. The proposed approach allows fast and reliable detection of acetaminophen in biological fluids with negligible matrix effect and remarkable reproducibility.",
publisher = "Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim",
journal = "Electroanalysis",
title = "Disposable Biosensor Based on Amidase/CeO2/GNR Modified Inkjet-printed CNT Electrodes-droplet Based Paracetamol Detection in Biological Fluids for “Point-of-care” Applications",
volume = "31",
number = "8",
pages = "1534-1542",
doi = "10.1002/elan.201900129"
}
Stanković, D., Ognjanović, M., Jović, M., Cuplić, V., Lesch, A., Girault, H. H., Gavrović-Jankulović, M.,& Antić, B. (2019). Disposable Biosensor Based on Amidase/CeO2/GNR Modified Inkjet-printed CNT Electrodes-droplet Based Paracetamol Detection in Biological Fluids for “Point-of-care” Applications.
ElectroanalysisWiley-VCH Verlag GmbH & Co. KGaA, Weinheim., 31(8), 1534-1542.
https://doi.org/10.1002/elan.201900129
Stanković D, Ognjanović M, Jović M, Cuplić V, Lesch A, Girault HH, Gavrović-Jankulović M, Antić B. Disposable Biosensor Based on Amidase/CeO2/GNR Modified Inkjet-printed CNT Electrodes-droplet Based Paracetamol Detection in Biological Fluids for “Point-of-care” Applications. Electroanalysis. 2019;31(8):1534-1542
Stanković Dalibor, Ognjanović Miloš, Jović Milica, Cuplić Valentina, Lesch Andreas, Girault Hubert H., Gavrović-Jankulović Marija, Antić Bratislav, "Disposable Biosensor Based on Amidase/CeO2/GNR Modified Inkjet-printed CNT Electrodes-droplet Based Paracetamol Detection in Biological Fluids for “Point-of-care” Applications" 31, no. 8 (2019):1534-1542,
https://doi.org/10.1002/elan.201900129 .
5
4
5

A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population

Tadić, D.; Popović, Milica; Gavrović-Jankulović, Marija; Đurić, Vojislav; Tomić-Špirić, Vesna; Rašković, Sanvila S.; Perić Popadić, Aleksandra

(Elsevier, 2019)

TY  - JOUR
AU  - Tadić, D.
AU  - Popović, Milica
AU  - Gavrović-Jankulović, Marija
AU  - Đurić, Vojislav
AU  - Tomić-Špirić, Vesna
AU  - Rašković, Sanvila S.
AU  - Perić Popadić, Aleksandra
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3728
AB  - Introduction: In the Serbian population allergy to weed pollen is the most common type of pollen-associated allergy, ahead of grass and tree pollens. Besides causing discomfort, allergy to pollen is often associated with rhinitis and asthma. Allergen-specific immunotherapy (ASIT) is the only treatment that can lead to potential long-term immune modification while reducing development of new sensitization and halting disease progression. The aim of the present study is to evaluate the efficacy of sublingual immunotherapy (SLIT) to weeds in the adult patient population using vaccine produced by the local Serbian Torlak Institute for virology, vaccines and serum. Methods: Adult patients with a clinical history of allergic rhinitis with and without asthma were included in the study. IgE-mediated sensitization to grass, tree and weed pollens was confirmed by skin prick testing and/or positive specific IgE. Patients were divided into two groups: patients with allergy to tree and grass pollen and patients with allergy to weeds. All patients received SLIT for three years, either with or without additional symptomatic therapy. Results: Three-year SLIT therapy led to significant improvement in several parameters, including skin-prick reactivity, decrease in specific IgE and use of symptomatic therapy, with mild adverse effects and high patient satisfaction concerning therapy. Conclusion: Three-year SLIT is a safe and efficient treatment option for respiratory allergy to weeds. Further observations in a larger number of patients could provide a better epidemiological evaluation of SLIT, but the positive effects we observed in our study may be considered representative despite the small number of patients.
PB  - Elsevier
T2  - Revue Francaise d'Allergologie
T1  - A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population
VL  - 59
IS  - 7
SP  - 474
EP  - 480
DO  - 10.1016/j.reval.2019.05.006
ER  - 
@article{
author = "Tadić, D. and Popović, Milica and Gavrović-Jankulović, Marija and Đurić, Vojislav and Tomić-Špirić, Vesna and Rašković, Sanvila S. and Perić Popadić, Aleksandra",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3728",
abstract = "Introduction: In the Serbian population allergy to weed pollen is the most common type of pollen-associated allergy, ahead of grass and tree pollens. Besides causing discomfort, allergy to pollen is often associated with rhinitis and asthma. Allergen-specific immunotherapy (ASIT) is the only treatment that can lead to potential long-term immune modification while reducing development of new sensitization and halting disease progression. The aim of the present study is to evaluate the efficacy of sublingual immunotherapy (SLIT) to weeds in the adult patient population using vaccine produced by the local Serbian Torlak Institute for virology, vaccines and serum. Methods: Adult patients with a clinical history of allergic rhinitis with and without asthma were included in the study. IgE-mediated sensitization to grass, tree and weed pollens was confirmed by skin prick testing and/or positive specific IgE. Patients were divided into two groups: patients with allergy to tree and grass pollen and patients with allergy to weeds. All patients received SLIT for three years, either with or without additional symptomatic therapy. Results: Three-year SLIT therapy led to significant improvement in several parameters, including skin-prick reactivity, decrease in specific IgE and use of symptomatic therapy, with mild adverse effects and high patient satisfaction concerning therapy. Conclusion: Three-year SLIT is a safe and efficient treatment option for respiratory allergy to weeds. Further observations in a larger number of patients could provide a better epidemiological evaluation of SLIT, but the positive effects we observed in our study may be considered representative despite the small number of patients.",
publisher = "Elsevier",
journal = "Revue Francaise d'Allergologie",
title = "A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population",
volume = "59",
number = "7",
pages = "474-480",
doi = "10.1016/j.reval.2019.05.006"
}
Tadić, D., Popović, M., Gavrović-Jankulović, M., Đurić, V., Tomić-Špirić, V., Rašković, S. S.,& Perić Popadić, A. (2019). A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population.
Revue Francaise d'AllergologieElsevier., 59(7), 474-480.
https://doi.org/10.1016/j.reval.2019.05.006
Tadić D, Popović M, Gavrović-Jankulović M, Đurić V, Tomić-Špirić V, Rašković SS, Perić Popadić A. A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population. Revue Francaise d'Allergologie. 2019;59(7):474-480
Tadić D., Popović Milica, Gavrović-Jankulović Marija, Đurić Vojislav, Tomić-Špirić Vesna, Rašković Sanvila S., Perić Popadić Aleksandra, "A real-life study of the efficacy of sublingual immunotherapy against weed allergies in the Serbian population" 59, no. 7 (2019):474-480,
https://doi.org/10.1016/j.reval.2019.05.006 .