Purification and characterization of a novel lignin peroxidase from white-rot fungus Phanerochaete sordida YK-624

被引：41
作者：
Sugiura, M [1 ]
Hirai, H [1 ]
Nishida, T [1 ]
机构：
[1] Shizuoka Univ, Fac Agr, Dept Forest Resources Sci, Shizuoka 4228529, Japan
来源：
FEMS MICROBIOLOGY LETTERS | 2003年 / 224卷 / 02期
关键词：
lignin peroxidase; sequential mechanism; lignin model compound; Phanerochaete sordida YK-624;
D O I：
10.1016/S0378-1097(03)00447-6
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
We characterized kinetics and substrate oxidation of a novel lignin peroxidase (YK-LiP) isolated from white-rot fungus Phanerochaete sordida YK-624. YK-LiP enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular mass of YK-LiP was approximately 50 kDa, and the absorption spectrum of YK-LiP was almost the same as that of the UP (Pc-LiP) from Phanerochaete chrysosporium. Steady-state kinetics of veratryl alcohol oxidation by YK-LiP (unlike that by Pc-LiP) revealed a bi-reactant sequential mechanism, although reactivity of YK-LiP to various monomeric substituted aromatic compounds was similar to that of Pc-LiP. Degradation of dimeric lignin model compounds was more effective by YK-LiP than by Pc-LiP, and the oxidation rate of sinapyl alcohol oligomer by YK-LiP was much faster than that by Pc-LiP. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码：285 / 290
页数：6
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