Molecular Cloning and Expression of a Novel Protease-resistant GH-36 alpha-Galactosidase from Rhizopus sp F78 ACCC 30795

文献类型： 外文期刊

第一作者： Yanan Cao

作者： Yanan Cao;Wang, Yaru;Luo, Huiying;Shi, Pengjun;Meng, Kun;Zhou, Zhigang;Yao, Bin;Zhang, Zhifang

作者机构：

关键词： alpha-Galactosidase;molecular cloning;Rhizopus sp F78;protease-resistant

期刊名称：JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：2.351； 五年影响因子：2.65 ）

ISSN： 1017-7825

年卷期： 2009 年 19 卷 11 期

页码：

收录情况： SCI

摘要： A 2,172-bp full-length gene (aga-F78), encoding a protease-resistant alpha-galactosidase, was cloned from Rhizopus sp. F78 and expressed in Escherichia coli. The deduced amino acid sequence shared highest identity (45.0%) with an alpha-galactosidase of glycoside hydrolase family 36 from Ahsidia corymbifera. After one-step purification with a Ni-NTA chelating column, the recombinant Aga-F78 migrated as a single band of similar to 82 and similar to 210 kDa on SDS-PAGE and nondenaturing gradient PAGE, respectively, indicating that the native structure of the recombinant Aga-F78 was a trimer. Exhibiting the similar properties as the authentic protein, purified recombinant Aga-F78 was optimally active at 50 degrees C and pH 4.8, highly pH stable over the pH range 5.0-10.0, more resistant to some cations and proteases, and had wide substrate specificity (pNPG, melidiose, raffinose, and stachyose). The recombinant enzyme also showed good hydrolytic ability to soybean meal, releasing galactose of 415.58 mu g/g soybean meal. When combined with trypsin, the enzyme retained over 90% degradability to soybean meal. These favorable properties make Aga-F78 a potential candidate for applications in the food and feed industries.

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