Preparation and characterization of stable cross-linked enzyme aggregates of novel laccase enzyme from Shewanella putrefaciens and using malachite green decolorization

被引：45
|
作者：
Sinirlioglu, Zeynep Aydin [1 ]
Sinirlioglu, Deniz [2 ]
Akbas, Fahri [1 ]
机构：
[1] Fatih Univ, Fac Engn, Dept Genet & Bioengn, TR-34500 Istanbul, Turkey
[2] Fatih Univ, Fac Art & Sci, Dept Chem, TR-34500 Istanbul, Turkey
来源：
BIORESOURCE TECHNOLOGY | 2013年 / 146卷
关键词：
Cross-linked enzyme aggregates; Decolorization; Cloning laccase enzyme; Shewanella putrefaciens; MULTICOPPER; PROTEINS; COPPER; CLEAS;
D O I：
10.1016/j.biortech.2013.08.032
中图分类号：
S2 [农业工程];
学科分类号：
0828 ;
摘要：
A novel type laccase from Shewanella putrefaciens was identified, expressed in Escherichia coli, characterized, prepared in cross-linked enzyme aggregates (CLEA) for industrial applications and investigated of decolorization activity on malchite green dye. Enzyme characterization was investigated by enzyme assay, SOS-PAGE and other biochemical reactions. Moreover, cross-linked enzyme aggregates were prepared and characterized. Saturated ammonium sulphate solution was used as the precipitating agent and cross linked with glutaraldehyde. These CLEA-laccase aggregates showed more catalytic efficiency and more stabilities compared to free laccase against harsh conditions of thermal and chemical agents as well as high reusability. Also it showed more decolorization ability. These results suggest that this CLEA is potentially usable in industrial applications. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码：807 / 811
页数：5
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