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Characterization and high expression of recombinant Ustilago maydis xylanase in Pichia pastoris

文献类型： 外文期刊

作者： Han, Hongjuan 1 ; You, Shuang 1 ; Zhu, Bo 1 ; Fu, Xiaoyan 1 ; Sun, Baihui 1 ; Qiu, Jin 1 ; Yu, Chengye 1 ; Chen, Lei 1 ; Pen 1 ;

作者机构： 1.Shanghai Acad Agr Sci, Agrobiotechnol Res Inst, Shanghai Key Lab Agr Genet & Breeding, Shanghai 201106, Peoples R China

2.Shanghai Acad Agr Sci, Agrobiotechnol Res Inst, Shanghai

关键词： Codon optimization;Enzyme characterization;High expression;Pichia pastoris;Xylanase

期刊名称：BIOTECHNOLOGY LETTERS （ 影响因子：2.461； 五年影响因子：2.457 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： A recombinant xylanase gene (rxynUMB) from Ustilago maydis 521 was expressed in Pichia pastoris, and the enzyme was purified and characterized. Phylogenetic analysis demonstrated that rxynUMB belongs to glycosyl hydrolase family 11. The Trp84, Trp95, Glu93, and Glu189 residues are proposed to be present at the active site. The apparent molecular mass of the recombinant xylananse was approximately 24 kDa, and the optimum pH and temperature were 4.3 and 50 A degrees C, respectively. Xylanase activity was enhanced by 166 and 115 % with Fe2+ and Mn2+, respectively. The biochemical properties of this recombinant xylanase suggest that it may be a useful candidate for a variety of commercial applications.

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