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[从本地枯草芽孢杆菌菌株OH67中克隆、表达新型漆酶并进行特性分析]

[Cloning, Expression, and Characterization of Novel Laccase Enzyme from Native Bacillus subtilis Strain OH67].

作者信息

Hajipour O, Mercan Dogan N, Dincer S, Norizadehazehkand M

机构信息

Department of Biology, Faculty of Science and Arts, Pamukkale University, Denizli, 20160 Turkey.

Department of Biology, Faculty of Science, Çukurova University, Adana, 01330 Turkey.

出版信息

Mol Biol (Mosk). 2020 Jul-Aug;54(4):680-687. doi: 10.31857/S0026898420040060.

DOI:10.31857/S0026898420040060
PMID:32799230
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.

摘要

细菌漆酶在高温和高pH值条件下非常稳定,并且具有许多生物技术和工业应用。在此我们描述了如何克隆、表达和纯化来自枯草芽孢杆菌的漆酶。在SDS-PAGE分析中,该酶的分子量被确定为34 kDa。重组酶的活性已通过愈创木酚氧化得以证明。该酶的KM值和Vmax值分别为1.1077 mM和19.3 μmol/分钟/毫克。重组漆酶对绿松石蓝HF6、雷马素红106、雷马素亮橙3R和亮蓝具有有效的脱色作用,因此,具备在纺织和环境工业中可能应用所需的特性。

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