A novel phytase with preferable characteristics from Yersinia intermedia

被引：83

作者：

Huang, Huoqing ^{[1
]}

Luo, Huiying ^{[1
]}

Yang, Peilong ^{[1
]}

Meng, Kun ^{[1
]}

Wang, Yaru ^{[1
]}

Yuan, Tiezheng ^{[1
]}

Bai, Yingguo ^{[1
]}

Yao, Bin ^{[1
]}

机构：

[1] Chinese Acad Sci, Dept Microbial Engn, Feed Res Inst, Beijing 100864, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 350卷 / 04期

关键词：

phytase; Yersinia intermedia; overexpression; characterization; Pichia pastoris;

D O I：

10.1016/j.bbrc.2006.09.118

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A Yersinia intermedia strain producing phytase was isolated from glacier soil. The phytase gene, appA, was isolated by degenerate PCR and TAIL-PCR. The full-length fragment contained 2354 bp with a 1326-bp open reading frame encoding 441 amino acids. APPA contained the active site RHGXRXP and HD sequence motifs that are typical of histidine acid phosphatases. To our knowledge, this is the first report of the detection of phytase activity and cloning of the relevant gene from Y. intermedia. The gene was overexpressed in Pichia pastoris, and the purified recombinant APPA had a specific activity for sodium phytate of 3960 U/mg, which is higher than that of the Citrobacter braakii phytase (previously the highest specific activity known). Recombinant APPA had high activity from pH 2 to 6 (optimum 4.5) and optimal temperature of 55 degrees C; the enzyme was resistant to pepsin and trypsin. These characteristics suggest that APPA may be highly suitable for use in the feed industry. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：884 / 889

页数：6

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