Đurđević Đelmaš, Aleksandra

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orcid::0000-0002-6951-4507
  • Đurđević Đelmaš, Aleksandra (5)
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Author's Bibliography

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" Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng. (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" Frontiers of Environmental Science & EngineeringFront. Environ. Sci. Eng., 15, no. 2 (2021):19,
https://doi.org/10.1007/s11783-020-1311-4 .
3
1

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

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

(Elsevier, 2020)

TY  - BOOK
AU  - Ilić Đurđić, Karla
AU  - Ostafe, Raluca
AU  - Đurđević Đelmaš, Aleksandra
AU  - Popović, Nikolina
AU  - Schillberg, Stefan
AU  - Fischer, Rainer
AU  - Prodanović, Radivoje
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3836
PB  - Elsevier
T2  - Enzyme and Microbial Technology
T1  - Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509
ER  - 
@book{
author = "Ilić Đurđić, Karla and Ostafe, Raluca and Đurđević Đelmaš, Aleksandra and Popović, Nikolina and Schillberg, Stefan and Fischer, Rainer and Prodanović, Radivoje",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3836",
publisher = "Elsevier",
journal = "Enzyme and Microbial Technology",
title = "Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509"
}
Ilić Đurđić, K., Ostafe, R., Đurđević Đelmaš, A., Popović, N., Schillberg, S., Fischer, R.,& Prodanović, R. (2020). Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509.
Enzyme and Microbial Technology
Elsevier..
Ilić Đurđić K, Ostafe R, Đurđević Đelmaš A, Popović N, Schillberg S, Fischer R, Prodanović R. Supplementary data for article: Ilić Đurđić, K.; Ostafe, R.; Đurđević Đelmaš, A.; Popović, N.; Schillberg, S.; Fischer, R.;  Prodanović, R. Saturation Mutagenesis to Improve the Degradation of Azo Dyes by Versatile Peroxidase and Application in Form of VP-Coated Yeast Cell Walls. Enzyme and Microbial Technology 2020, 136. https://doi.org/10.1016/j.enzmictec.2020.109509. 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" Enzyme and Microbial Technology (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 Technology
Elsevier., 136, e109509.
https://doi.org/10.1016/j.enzmictec.2020.109509
Ilić Đurđić K, Ostafe R, Đurđević Đelmaš A, Popović N, Schillberg S, Fischer R, Prodanović R. Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls. 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" Enzyme and Microbial Technology, 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 Technology
Elsevier., 136, e109509.
https://doi.org/10.1016/j.enzmictec.2020.109509
Ilić Đurđić K, Ostafe R, Đurđević Đelmaš A, Popović N, Schillberg S, Fischer R, Prodanović R. Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls. 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" Enzyme and Microbial Technology, 136 (2020):e109509,
https://doi.org/10.1016/j.enzmictec.2020.109509 .
8
4
5