TY  - JOUR
AU  - Ilic-Durdic, Karla
AU  - Ostafe, Raluca
AU  - Prodanović, Olivera
AU  - Durdevic-Delmas, Aleksandra
AU  - Popović, Nikolina
AU  - Fischer, Rainer
AU  - Schillberg, Stefan
AU  - Prodanović, Radivoje
PY  - 2021
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1488
AB  - The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) fromPhanerochaete chrysosporiumis 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 10(4) 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  - Higher Education Press, Beijing
T2  - Frontiers of Environmental Science & Engineering
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
IS  - 2
VL  - 15
DO  - 10.1007/s11783-020-1311-4
ER  - 

@article{
author = "Ilic-Durdic, Karla and Ostafe, Raluca and Prodanović, Olivera and Durdevic-Delmas, Aleksandra and Popović, Nikolina and Fischer, Rainer and Schillberg, Stefan and Prodanović, Radivoje",
year = "2021",
abstract = "The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods. Lignin peroxidase (LiP) fromPhanerochaete chrysosporiumis 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 10(4) 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 = "Higher Education Press, Beijing",
journal = "Frontiers of Environmental Science & Engineering",
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",
number = "2",
volume = "15",
doi = "10.1007/s11783-020-1311-4"
}

Ilic-Durdic, K., Ostafe, R., Prodanović, O., Durdevic-Delmas, A., Popović, N., Fischer, R., Schillberg, S.,& Prodanović, R.. (2021). Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering
Higher Education Press, Beijing., 15(2).
https://doi.org/10.1007/s11783-020-1311-4

Ilic-Durdic K, Ostafe R, Prodanović O, Durdevic-Delmas A, Popović N, Fischer R, Schillberg S, Prodanović R. Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls. in Frontiers of Environmental Science & Engineering. 2021;15(2).
doi:10.1007/s11783-020-1311-4 .

Ilic-Durdic, Karla, Ostafe, Raluca, Prodanović, Olivera, Durdevic-Delmas, Aleksandra, Popović, Nikolina, Fischer, Rainer, Schillberg, Stefan, Prodanović, Radivoje, "Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls" in Frontiers of Environmental Science & Engineering, 15, no. 2 (2021),
https://doi.org/10.1007/s11783-020-1311-4 . .