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

文献类型： 外文期刊

作者： Wang, Yue 1 ; Cao, Xueting 2 ; Jiang, Shanshan 1 ; Gao, Liwei 3 ; Han, Xiaolong 4 ; Qu, Jingyao 1 ; Jiang, Xukai 2 ; Liu, Guodong 1 ; Qu, Yinbo 1 ;

作者机构： 1.Shandong Univ, State Key Lab Microbial Technol, Qingdao 266237, Peoples R China

2.Shandong Univ, Natl Glycoengn Res Ctr, Shandong Key Lab Carbohydrate Chem & Glycobiol, NMPA Key Lab Qual Res & Evaluat Carbohydrate Based, Qingdao 266237, Peoples R China

3.Chinese Acad Agr Sci, Tobacco Res Inst, Qingdao 266101, Peoples R China

4.Jining Univ, Sch Life Sci & Bioengn, Jining 273155, Peoples R China

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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