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A Fungal alpha-Galactosidase from Tricholoma matsutake with Broad Substrate Specificity and Good Hydrolytic Activity on Raffinose Family Oligosaccharides

文献类型： 外文期刊

作者： Geng, Xueran 1 ; Tian, Guoting 2 ; Zhao, Yongchang 2 ; Zhao, Liyan 3 ; Wang, Hexiang 1 ; Ng, Tzi Bun 4 ;

作者机构： 1.China Agr Univ, Dept Microbiol, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China

2.Yunnan Acad Agr Sci, Inst Biotechnol & Germplasm Resource, Kunming 650223, Peoples R China

3.Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing 210095, Jiangsu, Peoples R China

4.Chinese Univ Hong Kong, Sch Biomed Sci, Fac Med, Shatin, Hong Kong, Peoples R China

关键词： mushroom;Tricholoma matsutake;alpha-galactosidase;characterization

期刊名称：MOLECULES （ 影响因子：4.411； 五年影响因子：4.587 ）

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收录情况： SCI

摘要： An acidic -galactosidase designated as TMG was purified from the fruiting bodies The purification protocol entailed ion exchange chromatography on Q-Sepharose and of Tricholoma matsutake with 136-fold purification and a specific activity of 909 units/mg. Mono-Q and fast protein liquid chromatography on Superdex 75. TMG is a monomeric protein exhibiting a molecular mass of 47 kDa in SDS-PAGE and gel filtration. The purified enzyme was identified by LC-MS/MS and three inner amino acid sequences were obtained. The optimum pH and temperature for TMG with pNPGal as substrate were pH 4.5 and 55 degrees C, respectively. The -galactosidase activity was strongly inhibited by K+, Ca2+, Cd2+, Hg2+, Ag+ and Zn2+ ions. The enzyme activity was inhibited by the chemical modification agent N-bromosuccinimide (NBS), indicating the importance of tryptophan residue(s) at or near the active site. Besides hydrolyzing pNPGal, TMG also efficaciously catalyzed the degradation of natural substrates such as stachyose, raffinose, and melibiose. Thus TMG can be exploited commercially for improving the nutritional value of soy milk by degradation of indigestible oligosaccharides.

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