Engineering mesophilic GH11 xylanase from Cellulomonas flavigena by rational design of N-terminus substitution.

ABSTRACT: Xylanase, a glycoside hydrolase, is widely used in the food, papermaking, and textile industries; however, most xylanases are inactive at high temperatures. In this study, a xylanase gene, CFXyl3, was cloned from Cellulomonas flavigena and expressed in Escherichia coli BL21 (DE3). To improve the thermostability of xylanase, four hybrid xylanases with enhanced thermostability (designated EcsXyl1-4) were engineered from CFXyl3, guided by primary and 3D structure analyses. The optimal temperature of CFXyl3 was improved by replacing its N-terminus with the corresponding area of SyXyn11P, a xylanase that belongs to the hyperthermostable GH11 family. The optimal temperatures of the hybrid xylanases EcsXyl1-4 were 60, 60, 65, and 85°C, respectively. The optimal temperature of

SUBMITTER: Tian W 

PROVIDER: S-EPMC9669568 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature