Functional Analysis of a Highly Active beta-Glucanase from Bispora sp MEY-1 Using Its C-terminally Truncated Mutant

文献类型： 外文期刊

第一作者： You, Shuai

作者： You, Shuai;Tu, Tao;Ma, Rui;Huang, Huo-qing;Wang, Yuan;Bai, Ying-guo;Su, Xiao-yun;Cai, Hui-yi;Yao, Bin;Luo, Hui-ying

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关键词： Bispora sp MEY-1; beta-1,3-1,4-glucanase; serine/proline-rich module; glycoside hydrolase (GH) family 16; broad substrate specificity

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2018 年 66 卷 37 期

页码：

收录情况： SCI

摘要： A beta-1,3-1,4-glucanase-encoding gene, Bisglul6B, was identified in Bispora sp. MEY-1. The deduced BisG1u16B consists of an N-terminal signal peptide, a catalytic module of glycoside hydrolase family 16 (GH16), and a C-terminal serine/proline-rich module. After expression in Pichia pastoris GS115, the purified recombinant BisGlul6B showed maximal activity at pH 4.0 and 55 degrees C and had broad substrate specificity (beta-1,3-/beta-1,4-mixed, beta-1,3-, beta-1,4-, and beta-1,6-linked glucan, and beta-1,4-mannan). The enzyme possessed high specific activities toward barley beta-glucan (34 700 U center dot mg(-1)), lichenan (23 900 U center dot mg(-1)), and laminarin (9 000 U center dot g(-1)). After removing the C-terminal module, the truncated mutant, BisG1u16B-Delta C, retained similar enzymatic properties to the wild type but displayed significantly enhanced activities (up to 2.5-fold). Functional and structural analyses indicated that the C-terminal module plays a key role in the substrate binding of BisGlul6B. This study provided an excellent candidate glucanase for industrial purposes and revealed the functions of a C-terminal serine/proline-rich region.

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