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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
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
更新日期:2020-08-19
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