Characterization of Trametes versicolor laccase for the transformation of aqueous phenol

被引：120
|
作者：
Kurniawati, Selvia [1 ]
Nicell, James A. [1 ]
机构：
[1] McGill Univ, Dept Civil Engn & Appl Mech, Montreal, PQ H3A 2K6, Canada
来源：
BIORESOURCE TECHNOLOGY | 2008年 / 99卷 / 16期
基金：
加拿大自然科学与工程研究理事会;
关键词：
laccase; inactivation; phenol; oxidation; enzyme;
D O I：
10.1016/j.biortech.2008.01.084
中图分类号：
S2 [农业工程];
学科分类号：
0828 ;
摘要：
Laccase (oxygen oxidoreductase, EC 1.10.3.2) from Trametes versicolor was thoroughly characterized in terms of its catalytic stability and its effectiveness as a biocatalyst under various reaction conditions when using phenol as a model substrate. This enzyme demonstrated high or moderate degrees of stability at pHs from 5 to 8 at 25 degrees C and at temperatures from 10 to 30 degrees C at pH 6. Exponential decay expressions were successfully used to model laccase inactivation when incubated under various conditions of pH and temperature. Phenol transformation was optimum at pH 6, but significant transformation was observed over a pH range of 4-7, provided that sufficient laccase was present in the reacting solution. Partial inactivation of laccase was observed during the oxidation of phenol, even under conditions of optimal stability (pH 6 and 25 degrees C). (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码：7825 / 7834
页数：10
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