Molecular Characterization of a Highly-Active Thermophilic beta-Glucosidase from Neosartorya fischeri P1 and Its Application in the Hydrolysis of Soybean Isoflavone Glycosides

文献类型： 外文期刊

第一作者： Yang, Xinzhuo

作者： Yang, Xinzhuo;Ma, Rui;Shi, Pengjun;Huang, Huoqing;Bai, Yingguo;Wang, Yaru;Yang, Peilong;Yao, Bin;Ma, Rui;Fan, Yunliu

作者机构：

期刊名称：PLOS ONE （ 影响因子：3.24； 五年影响因子：3.788 ）

ISSN： 1932-6203

年卷期： 2014 年 9 卷 9 期

页码：

收录情况： SCI

摘要： Isoflavone occurs abundantly in leguminous seeds in the form of glycoside and aglycone. However, isoflavone glycoside has anti-nutritional effect and only the free type is beneficial to human health. In the present study we identified a beta-glucosidase from thermophilic Neosartorya fischeri P1, termed NfBGL1, capable of efficiently converting isoflavone glycosides into free isoflavones. The gene, belonging to glycoside hydrolase family 3, was successfully overexpressed in Pichia pastoris at high cell density in a 3.7-l fermentor. Purified recombinant NfBGL1 had higher specific activity (2189 +/- 1.7 U/mg) and temperature optimum (80 degrees C) than other fungal counterparts when using p-nitrophenyl beta-D-glucopyranoside as the substrate. It retained stable at temperatures up to 70 degrees C and over a broad pH range of 3.0-10.0. NfBGL1 had broad substrate specificity including glucosidase, cellobiase, xylanase and glucanase activities, and displayed preference for hydrolysis of beta-1,2 glycosidic bond rather than beta-1,3, beta-1,4, beta-1,6 bonds. The enzyme showed high bioconversion ability for major soybean isoflavone glycosides (daidin, gensitin and glycitin) into free forms. These properties make NfBGL1 potential for the wide use in the food, feed, pharmacy and biofuel industries.

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