Comparative characterization of four laccases from Trametes versicolor concerning phenolic C-C coupling and oxidation of PAHs

被引：62

作者：

Koschorreck, Katja ^{[1
]}

Richter, Sven M. ^{[1
]}

Swierczek, Andre ^{[2
]}

Beifuss, Uwe ^{[2
]}

Schmid, Rolf D. ^{[1
]}

Urlacher, Vlada B. ^{[1
]}

机构：

[1] Univ Stuttgart, Inst Tech Biochem, D-70569 Stuttgart, Germany

[2] Univ Hohenheim, Inst Chem, D-70599 Stuttgart, Germany

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2008年 / 474卷 / 01期

关键词：

laccase; Tramates versicolor; polycyclic aromatic hydrocarbons; oxidation; C-C coupling; site-directed mutagenesis;

D O I：

10.1016/j.abb.2008.03.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The laccase genes Icc alpha, Icc beta, Icc gamma and Icc delta encoding four isoenzymes from Trametes versicolor have been cloned and expressed in Pichia pastoris. Biochemical characterization allowed classification of these laccases into two distinct groups: Lcc alpha and Lcc beta possessed higher thermal stability, but lower catalytic activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulpbonic acid) (ABTS) compared to Lcc gamma and Lcc delta. Activities of the laccases were quite different as well. Laccase Lcc delta showed highest phenolic C-C coupling activity with sinapic acid, but lowest oxidizing activity towards polycyclic aromatic hydrocarbons (PAHs). Highest activity towards PAHs was observed with Lcc beta. After 72 h, more than 80% of fluorene, anthracene, acenaphthene and acenaphthylene were oxidized by Lcc beta in the presence of ABTS. Investigation of the structural basis of the different activities of the laccases demonstrated the impact of positions 164 and 265 in the substrate binding site on oxidation of PAHs. (C) 2008 Elsevier Inc. All rights reserved

引用

页码：213 / 219

页数：7

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