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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