A thermophilic and acid stable family-10 xylanase from the acidophilic fungus Bispora sp MEY-1

文献类型： 外文期刊

第一作者： Luo, Huiying

作者： Luo, Huiying;Yang, Jun;Wang, Hui;Yang, Yuhui;Huang, Huoqing;Shi, Pengjun;Yuan, Tiezheng;Yao, Bin;Li, Jiang;Fan, Yunliu

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关键词： Thermophilic xylanase;Acidophilic fungus;Bispora sp MEY-1;Pichia pastoris

期刊名称：EXTREMOPHILES （ 影响因子：2.395； 五年影响因子：2.668 ）

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收录情况： SCI

摘要： A complete gene, xyl10C, encoding a thermophilic endo-1,4-beta-xylanase (XYL10C), was cloned from the acidophilic fungus Bispora sp. MEY-1 and expressed in Pichia pastoris. XYL10C shares highest nucleotide and amino acid sequence identities of 57.3 and 49.7%, respectively, with a putative xylanase from Aspergillus fumigatus Af293 of glycoside hydrolase family 10. A high expression level in P. pastoris (73,400 U ml(-1)) was achieved in a 3.7-l fermenter. The purified recombinant XYL10C was thermophilic, exhibiting maximum activity at 85A degrees C, which is higher than that reported from any fungal xylanase. The enzyme was also highly thermostable, exhibiting root similar to 100% of the initial activity after incubation at 80A degrees C for 60 min and > 87% of activity at 90A degrees C for 10 min. The half lives of XYL10C at 80 and 85A degrees C were approximately 45 and 3 h, respectively. It had two activity peaks at pH 3.0 and 4.5-5.0 (maximum), respectively, and was very acid stable, retaining more than 80% activity after incubation at pH 1.5-6.0 for 1 h. The enzyme was resistant to Co2+, Mn2+, Cr3+ and Ag+. The specific activity of XYL10C for oat spelt xylan was 18,831 U mg(-1). It also had wide substrate specificity and produced simple products (65.1% xylose, 25.0% xylobiose and 9.9% xylan polymer) from oat spelt xylan.

分类号： Q93

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