Purification and characterization of a novel protease-resistant alpha-galactosidase from Rhizopus sp. F78 ACCC 30795

文献类型： 外文期刊

第一作者： Cao, Yanan

作者： Cao, Yanan;Yang, Peilong;Shi, Pengjun;Wang, Yaru;Luo, Huiying;Meng, Kun;Zhang, Zhifang;Wu, Ningfeng;Yao, Bin;Fan, Yunliu

作者机构：

关键词： Alpha-galactosidase;Rhizopus sp.;Characterization;Protease resistant

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

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收录情况： SCI

摘要： A novel extracellular a-galactosidase, named Aga-F78, from Rhizopus sp. F78 ACCC 30795 was induced, purified and characterized in this study. This soybean-inducible a-galactosidase was purified to homogeneity by ammonium sulfate precipitation and fast protein liquid chromatography (FPLC), with a yield of 14.6% and a final specific activity of 74.6 U mg~(-1). Aga-F78 has an estimated relative molecular mass of 78 kDa from SDS-PAGE while native mass of 210 kDa and 480 kDa from non-denaturing gradient PAGE. This alpha-galactosidase had no N- or O-glycosylated. Amino acid sequences of three internal fragments were determined, and fragment 1, NQLVLDLTR, shared high homology with bacterial and fungal GH-36 alpha-galactosidases. The optimum pH and temperature on activity of Aga-F78 were 4.8 and 50 deg C, respectively. The properties of pH and temperature stability, effect of ions and chemicals were also studied. Furthermore, the resistant to neutral and alkaline proteases and substrate specificity of natural substrates (melibiose, raffinose, stachyose and guar gum) were also studied to enlarged the application of Aga-F78 in more fields. Kinetic studies revealed a K_m and V_(max) of 2.9 mmol l~(-1) and 246.1 mu mol (mg min)~(-1), respectively, using pNPG as substrate. To our knowledge, this is the first report of purification and characterization of alpha-galactosidase from Rhizopus with some special properties, which may aid its utilization in the food and feed industries.

分类号： Q55

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