Properties of a novel alpha-galactosidase from Streptomyces sp. S27 and its potential for soybean processing

文献类型: 外文期刊

第一作者: Cao, Yanan

作者: Cao, Yanan;Yuan, Tiezheng;Shi, Pengjun;Luo, Huiying;Li, Ning;Meng, Kun;Bai, Yingguo;Yang, Peilong;Zhou, Zhigang;Yao, Bin;Zhang, Zhifang

作者机构:

关键词: alpha-Galactosidase;Streptomyces;Overexpression;High hydrolytic activity;Raffinose family oligosaccharides (RFOs)

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: 2010 年 47 卷 7 期

页码:

收录情况: SCI

摘要: A full-length alpha-galactosidase gene (2226 bp) was cloned from Streptomyces sp. S27 ACCC 41168 and overexpressed in Escherichia coli. The deduced amino acid sequence shared highest identities of 82% with a putative alpha-galactosidase from Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111 and 46% with a known alpha-galactosidase from Bifidobacteriurn bifidum NCIMB 41171, both of which belong to glycoside hydrolase (CH) family 36. The purified recombinant enzyme showed a single protein band of similar to 82 kDa on SDS-PAGE and three bands of similar to 220, 320 and 480 kDa on non-denaturing gradient PAGE, respectively, indicating its native structure of trimer, tetramer or hexamer. The enzyme exhibited optimal activity at conditions of 35 degrees C and pH 7.4. similar to the intestinal conditions of mammals and poultry, was resistant to some neutral proteases (alpha-chymotrypsin, subtilisin A and collagenase), and showed hydrolytic ability to natural substrates, including melibiose, stachyose, raffinose and soybean meal. When combined with intestinal proteases, the enzyme showed higher hydrolytic ability to raffinose family oligosaccharides (RFOs) in soybean product. These favorable properties make the Streptomyces sp. S27 alpha-galactosidase very prospective in soybean processing for food and feed industries. (C) 2010 Elsevier Inc. All rights reserved.

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