Engineering the substrate preference of glucose oxidase for the enzymatic oxidation of xylose

文献类型： 外文期刊

第一作者： Wang, Yue

作者： Wang, Yue;Jiang, Shanshan;Qu, Jingyao;Liu, Guodong;Qu, Yinbo;Cao, Xueting;Jiang, Xukai;Liu, Guodong;Qu, Yinbo;Gao, Liwei;Han, Xiaolong

作者机构：

期刊名称：GREEN CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.8 ）

ISSN： 1463-9262

年卷期： 2024 年 26 卷 8 期

页码：

收录情况： SCI

摘要： Glucose oxidase (GOx) catalyzes the oxidation of d-glucose to d-glucono-1,5-lactone and has a wide range of applications in various industries. However, the strict substrate specificity of GOx hampers its application in the conversion of other abundant sugars such as d-xylose. In this study, the substrate preference of GOx from Aspergillus niger (AnGOx) was engineered using a semi-rational design approach. The mutant T110V/F414L exhibited a 5.7-fold increase in d-xylose oxidation activity compared to that of the wild-type enzyme, which was attributed to its enhanced affinity for the substrate. Molecular dynamics simulations indicated that the T110V and F414L mutations may mitigate the non-productive binding of d-xylose at the entrance of the substrate-binding pocket, and therefore, are beneficial for providing access of its C1 hydroxyl group to the catalytic residues. Moreover, the mutant simultaneously oxidized d-xylose and d-glucose in the corncob hydrolysate to the corresponding aldonic acids when coupled with catalase. These findings provide new insights into substrate recognition by GOx and offer a new method for the utilization of d-xylose from lignocellulosic feedstocks. Glucose oxidase was engineered for increased activity on d-xylose, which enabled co-oxidation of d-glucose and d-xylose to corresponding aldonolactones.

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