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Construction, expression and characterization of fusion enzyme containing azoreductase and glucose 1-dehydrogenase for dye removal

文献类型： 外文期刊

作者： Lu, Li-Ling 1 ; Yang, Yu-Yi 2 ; Lin, Hui 3 ; Gao, Fen 1 ; Zhao, Yu-Hua 1 ;

作者机构： 1.Zhejiang Univ, Coll Life Sci, Hangzhou 310058, Zhejiang, Peoples R China

2.Chinese Acad Sci, Wuhan Bot Garden, Key Lab Aquat Bot & Watershed Ecol, Wuhan 430074, Peoples R China

3.Zhejiang Acad Agr Sci, Inst Environm Resource Soil & Fertilizer, Hangzhou 310000, Zhejiang, Peoples R China

关键词： Fusion enzyme;Azoreductase;Glucose 1-dehydrogenase;NADH;Cyclic utilization

期刊名称：INTERNATIONAL BIODETERIORATION & BIODEGRADATION （ 影响因子：4.32； 五年影响因子：4.719 ）

ISSN： 0964-8305

年卷期： 2014 年 87 卷

页码：

收录情况： SCI

摘要： Azoreductase (AZR) has been found to be an effective enzyme for azo dye removal. However, NAD(P)H is required as electron donor for the cleavage of the azo bond by AZR. Due to the high cost of the reduced nicotinamide coenzyme, the large scale application of AZR is impractical. In this study, an artificial fusion enzyme of azoreductase and alkaline-resistant NAD(P)-dependent glucose 1-dehydrogenase (LsGDH) called GFA was constructed for NAD(P)H regeneration and cyclic utilization. The purified fusion enzyme migrated as a single protein band on SDS-PAGE with a molecular weight of similar to 55 kDa, exhibiting both azoreductase and glucose 1-dehydrogenase activities. The azoreductase moiety of the fusion enzyme exhibited high enzyme activities towards Methyl Red (160.62 U mg(-1)), which was slightly higher than parental azoreductase (153.16 U mg(-1)). Compared with parental enzymes, the azoreductase moiety was characterized by kinetic parameters of decreased K-m (0.52-fold) and increased K-cat (1.25-fold). These indicate a 2.41-fold net increase in catalytic efficiency (K-cat/K-m) of the azoreductase moiety. The highest enzymatic degradation was achieved at the temperature of 45 degrees C and pH of 7.0, respectively. Mg2+ and Ca2+ enhanced the fusion enzyme activity, while Cr2+, Mn2+ and Zn2+ inhibited the activity to varying extents. The enzyme activity of the fusion enzyme was enhanced by low concentrations of dodecyl trimethyl ammonium bromide (DTAB) and cetylpyridinium chloride (CPC) but inhibited by high concentrations of surfactants. (C) 2013 Elsevier Ltd. All rights reserved.

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