A New alpha-Galactosidase from Thermoacidophilic Alicyclobacillus sp A4 with Wide Acceptor Specificity for Transglycosylation

文献类型： 外文期刊

第一作者： Wang, Huimin

作者： Wang, Huimin;Ma, Rui;Shi, Pengjun;Xue, Xianli;Luo, Huiying;Huang, Huoqing;Bai, Yingguo;Yang, Peilong;Yao, Bin

作者机构：

关键词： alpha-Galactosidase;Alicyclobacillus sp A4;Transglycosylation;Wide acceptor specificity

期刊名称：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：2.926； 五年影响因子：2.685 ）

ISSN： 0273-2289

年卷期： 2014 年 174 卷 1 期

页码：

收录情况： SCI

摘要： An alpha-galactosidase gene (gal36A4) of glycosyl hydrolase family 36 was identified in the genome of Alicyclobacillus sp. A4. It contains an ORF of 2,187 bp and encodes a polypeptide of 728 amino acids with a calculated molecular mass of 82.6 kDa. Deduced Gal36A4 shows the typical GH36 organization of three domains-the N-terminal beta-sheets, the catalytic (beta/alpha)(8)-barrels, and the C-terminal antiparallel beta-sheet. The gene product was produced in Escherichia coli and showed both hydrolysis and transglycosylation activities. The optimal pH for hydrolysis activity was 6.0, and a stable pH range of 5.0-11.0 was found. The enzyme had a temperature optimum of 60 A degrees C. It is specific for alpha-1,6-glycosidic linkages and had a K (m) value of 1.45 mM toward pNPGal. When using melibiose as both donor and acceptor of galactose, Gal36A4 showed the transfer ratio of 23.25 % at 96 h. With respect to acceptor specificity, all tested monosaccharides, disaccharides, and oligosaccharides except for D-xylose and L-arabinose were good acceptors for transglycosylation. Thus, Gal36A4 may find diverse applications in industrial fields, especially in the food industry.

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