数字农科院2.0

High-level expression of a novel Penicillium endo-1,3(4)-beta-D-glucanase with high specific activity in Pichia pastoris

文献类型： 外文期刊

作者： Chen, Xiaoyan;Meng, Kun;Shi, Pengjun;Bai, Yingguo;Luo, Huiying;Huang, Huoqing;Yuan, Tiezheng;Yang, Peilong;Yao, Bin

作者机构：

关键词： Penicillium pinophilum C1;Endo-1;3(4)-β-glucanase;Pichia pastoris;Overexpression;High specific activity

期刊名称： JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY

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收录情况： SCI

摘要： A novel endo-1,3(4)-beta-d-glucanase gene (bgl16C1) from Penicillium pinophilum C1 was cloned and sequenced. The 945-bp full-length gene encoded a 315-residue polypeptide consisting of a putative signal peptide of 18 residues and a catalytic domain belonging to glycosyl hydrolase family 16. The deduced amino acid sequence showed the highest identity (82%) with the putative endo-1,3(4)-beta-glucanase from Talaromyces stipitatus ATCC 10500 and 60% identity with the characterized beta-1,3(4)-glucanase from Paecilomyces sp. FLH30. The gene was successfully overexpressed in Pichia pastoris. Recombinant Bgl16C1 constituted 95% of total secreted proteins (2.61 g l(-1)) with activity of 28,721 U ml(-1) in a 15-l fermentor. The purified recombinant Bgl16C1 had higher specific activity toward barley beta-glucan (12,622 U mg(-1)) than all known glucanases and also showed activity against lichenan and laminarin. The enzyme was optimally active at pH 5.0 and 55A degrees C and exhibited good stability over a broad acid and alkaline pH range (> 85% activity at pH 3.0-7.0 and even 30% at pH 11.0). All these favorable enzymatic properties make it attractive for potential applications in various industries.

分类号： Q81

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