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Cloning, Expression, and Characterization of Novel Laccase Enzyme from Native Bacillus subtilis Strain OH67
Molecular Biology ( IF 1.5 ) Pub Date : 2020-08-19 , DOI: 10.1134/s0026893320040068
O. Hajipour , N. Mercan Dogan , S. Dincer , M. Norizadehazehkand

Abstract

Bacterial laccases are very stable at high temperature and high pH values, and have many biotechnological and industrial applications. Here we describe how we cloned, expressed and purified the laccase from Bacillus subtilis (B. subtilis). The enzyme molecular weight has been determined as 34 kDa in SDS- PAGE analysis. The activity of the recombinant enzyme has been proved by guaiacol oxidation. The KM and Vmax values of the enzyme were at 1.1077 mM and at 19.3 µmol/min/mg, respectively. The recombinant laccase was effective in the decolorization of Turquoise blue HF6, Remazol red 106, Remazol brilliant orange 3R, and Brilliant blue, thus, possessing the characteristics necessary for its possible application in textile and environmental industries.


中文翻译:

天然枯草芽孢杆菌菌株OH67新型漆酶的克隆,表达及鉴定

摘要

细菌漆酶在高温和高pH值下非常稳定,并具有许多生物技术和工业应用。在这里,我们描述了如何从枯草芽孢杆菌B.subtilis)中克隆,表达和纯化漆酶在SDS-PAGE分析中,酶分子量已确定为34 kDa。愈创木酚氧化已证明了重组酶的活性。该ķ中号V最大该酶的值分别为1.1077mM和19.3μmol/ min / mg。重组漆酶对绿松石蓝HF6,Remazol红106,Remazol亮橙3R和亮蓝的脱色有效,因此具有在纺织和环境工业中可能应用的必要特性。
更新日期:2020-08-19
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