Results 1 to 10 of about 42 (36)
Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17 [PDF]
Background Dye-decolorizing peroxidases (DyPs) represent a novel family of heme peroxidases that use H2O2 as the final electron acceptor to catalyze the oxidation of various organic compounds.
Liuqing Li +6 more
doaj +5 more sources
Genome sequence of the white-rot fungus Irpex lacteus F17, a type strain of lignin degrader fungus [PDF]
Irpex lacteus, a cosmopolitan white-rot fungus, degrades lignin and lignin-derived aromatic compounds. In this study, we report the high-quality draft genome sequence of I.
Mengwei Yao +4 more
doaj +5 more sources
Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete [PDF]
Irpex lacteus F17 is well-known for its ability to degrade recalcitrant aromatic pollutants, which mainly results from the action of the manganese peroxidase (MnP) that it is able to produce.
Zihong Duan +4 more
doaj +5 more sources
Il-DyP4, a dye-decolorizing peroxidase (DyP) from Irpex lacteus F17, has a strong ability to oxidise harmful aromatic compounds, implying application potential in the field of environmental protection. However, the low H2O2 stability of Il-DyP4 hinders its practical application.
Huang, Wenhan +3 more
openaire +1 more source
Additional file 1: Table S1 The primers sequences used in this study. Table S2 The structures of substrates used in this study. Fig. S1 Sequence alignments of tryptophan and tyrosine residues in Il-DyP4 with other representative class V DyPs. Highlighted residues include the following: (i) tryptophan residues were shown in red and the corresponding ...
Li, Liuqing +6 more
openaire +1 more source
Caragana korshinskii kom. (CKK) waste, a common forestry byproduct in northwest of China, presents challenges in its transformation into alternative ruminant feed due to its initial nutritional limitations and unappealing palatability.
Guilin Du +7 more
doaj +1 more source
Gene contents in oxidoreductases, secreted proteases and secondary metabolism in the genomes of I. lacteus F17. (DOCX 15Â kb)
Mengwei Yao +4 more
openaire +1 more source
Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates. [PDF]
de Eugenio LI +6 more
europepmc +1 more source
Textile Dye Biodecolorization by Manganese Peroxidase: A Review. [PDF]
Chang Y, Yang D, Li R, Wang T, Zhu Y.
europepmc +1 more source

