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Fermentation Production, Purification and Characterization of a Fungal alpha-galactosidase from Trametes versicolor and Its Synergistic Degradation of Guar Gum with Mannanase

文献类型： 外文期刊

作者： Liu, Qin 1 ; Du, Fang 2 ; Kong, Weili 1 ; Wang, Hexiang 3 ; Ng, Tzi Bun 5 ;

作者机构： 1.Henan Acad Agr Sci, Inst Plant Nutr Agr Resources & Environm Sci, Zhengzhou 450002, Peoples R China

2.Chinese Acad Agr Sci, Inst Agr Resources & Reg Planning, Beijing 100081, Peoples R China

3.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China

4.China Agr Univ, Dept Microbiol, Beijing 100193, Peoples R China

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

关键词： medium optimization; alpha-galactosidase; Trametes versicolor; characterization; synergistic effect

期刊名称：FOOD SCIENCE AND TECHNOLOGY RESEARCH （ 影响因子：0.668； 五年影响因子：0.895 ）

ISSN： 1344-6606

年卷期： 2020 年 26 卷 2 期

页码：

收录情况： SCI

摘要： The optimization of fermentation medium for alpha-galactosidase production by Trametes versicolor was investigated by using orthogonal design in shaker flask fermentation. The optimal liquid medium for alpha-galactosidase production by T. versicolor was consist of 1.0 % soybean cake power, 0.60 % galactose, 0.15 % KH 2PO4, 0.09 % MgSO4. Then, the alpha-galactosidase from T. versicolor (TVG) was purified and characterized. The purified enzyme, a monomeric protein with a molecular weight of 70 kDa, was purified 332-fold by means of ion exchange chromatography and gel filtration. The optimal pH and temperature of TVG with p-nitro-phenyl alpha-D-galactopyranoside (pNPG) as substrate were 3.0 and 60 degrees C, respectively. The activity of TVG was inhibited by N-bromosuccinimide (NBS), constituting evidence for the essentiality of tryptophan residue(s) at or in the vicinity of the active centre. The alpha-galactosidase presented a broad substrate specificity, which included pNPG, melibiose, raffinose, and stachyose with K-m values of 0.651, 3.66, 15.1, and 4.47 mM, correspondingly. Galactose acted as a noncompetitive inhibitor with K-i and K-is of 2.88 and 0.132 mM, respectively. A synergistic acceleration in guar gum degradation was found when TVG and mannanase were combined.

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