LIGNIN-DEGRADING PEROXIDASES OF PHANEROCHAETE-CHRYSOSPORIUM

被引：37

作者：

CAI, DY ^{[1
]}

TIEN, M ^{[1
]}

机构：

[1] PENN STATE UNIV,DEPT MOLEC & CELL BIOL,UNIV PK,PA 16802

来源：

JOURNAL OF BIOTECHNOLOGY | 1993年 / 30卷 / 01期

关键词：

LIGNINASE; FUNGI; ENZYME;

D O I：

10.1016/0168-1656(93)90029-M

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by which they oxidize substrates also appears to be the similar. pH has a similar effect on lignin peroxidase compound I formation as on HRP or CcP; however, the pK(a) controlling compound I formation for lignin peroxidase appears to be much lower. Lignin-degrading peroxidases are able to catalyze the oxidation of substrates with high redox potential. This unique ability is consistent with a heme active site of low electron density, which is indicated by high redox potential.

引用

页码：79 / 90

页数：12

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