A highly pH-stable phytase from Yersinia kristeensenii: Cloning, expression, and characterization

文献类型： 外文期刊

第一作者： Fu, Dawei

作者： Fu, Dawei;Huang, Huoqing;Luo, Huiying;Wang, Yaru;Yang, Peilong;Meng, Kun;Bai, Yingguo;Yao, Bin;Wu, Ningfeng

作者机构：

关键词： phytase;pH stable;histidine acid phosphatase;Yersinia kristeensenii;Pichia pastoris

期刊名称：ENZYME AND MICROBIAL TECHNOLOGY （ 影响因子：3.493； 五年影响因子：3.699 ）

ISSN： 0141-0229

年卷期： 2008 年 42 卷 6 期

页码：

收录情况： SCI

摘要： The gene appA, encoding a phytase from Yersinia kristeensenii, was cloned and heterologously expressed in Pichia pastoris. The open reading frame of appA comprised 1326 bp encoding a protein of 441 amino acids including a 24-amino acid signal peptide. The encoded phytase, APPA, was 87% identical to the phytase from Y. intermedia but was <52% identical to other histidine acid phosphatases. The purified recombinant phytase had an optimal activity at 55 degrees C and pH 4.5, and it exhibited enzymatic activity between pH 2.0 and 6.5, with a specific activity of 2656 U mg(-1) at pH 4.5 and 37 degrees C. r-APPA retained more than 90% of its initial activity after being incubated under varying pH conditions (pH 1.5-11.0) at 37 degrees C for 3 h. r-APPA was resistant to heat inactivation, as it retained 46% of its initial activity after incubation at 80 degrees C for 10 min. r-APPA was effective for the hydrolysis of phytate phosphorus from soybean meal in vitro. Comparison of r-APPA with other well-known phytases suggests that the Y kristeensenii phytase would be an attractive enzyme for feed industry use. (C) 2008 Elsevier Inc. All rights reserved.

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