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Engineering the substrate preference of glucose oxidase for the enzymatic oxidation of xylose.
- Source :
-
Green Chemistry . 4/21/2024, Vol. 26 Issue 8, p4851-4859. 9p. - Publication Year :
- 2024
-
Abstract
- 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 14639262
- Volume :
- 26
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Green Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 176761530
- Full Text :
- https://doi.org/10.1039/d3gc04981g