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High expression of recombinant Streptomyces sp S38 xylanase in Pichia pastoris by codon optimization and analysis of its biochemical properties

文献类型： 外文期刊

作者： Fu, Xiao-Yan 1 ; Zhao, Wei 1 ; Xiong, Ai-Sheng 1 ; Tian, Yong-Sheng 1 ; Peng, Ri-He 1 ;

作者机构： 1.Shanghai Acad Agr Sci, Agrobiotechnol Res Inst, Shanghai 201106, Peoples R China

关键词： potassium ion: 24203-36-9;copper(II) ion: 15158-11-9;calcium ion: 14127-61-8;chromium(III) ion: 16065-83-1;AOX1 promoter;xylanase: 37278-89-0;EC 3.2.1.32;recombinant;inhibition;activity;enzyme activity;biochemical property

期刊名称：MOLECULAR BIOLOGY REPORTS （ 影响因子：2.316； 五年影响因子：2.357 ）

ISSN：

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收录情况： SCI

摘要： In recent years, the biotechnological use of xylanases has grown remarkably. To efficiently produce xylanase for food processing and other industry, a codon-optimized recombinant xylanase gene from Streptomyces sp. S38 was synthesized and extracellularly expressed in Pichia pastoris under the control of AOX1 promoter. SDS-PAGE and activity assay demonstrated that the molecular mass of the recombinant xylanase was estimated to be 25 kDa, the optimum pH and optimum temperature were 5.5 and 50A degrees C, respectively. In shake flask culture, the specific activity of the xylanase activity was 5098.28 U/mg. The K (m) and V (max) values of recombinant xylanase were 11.0 mg/ml and 10000 mu mol min(-1) mg(-1), respectively. In the presence of metal ions such as Ca2+, Cu2+, Cr3+ and K+, the activity of the enzyme increased. However, strong inhibition of the enzyme activity was observed in the presence of Hg2+. This is the first report on the expression properties of a recombinant xylanase gene from the Streptomyces sp. S38 using Pichia pastoris. The attractive biochemical properties of the recombinant xylanase suggest that it may be a useful candidate for variety of commercial applications.

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