Activity and Thermostability of GH5 Endoglucanase Chimeras from Mesophilic and Thermophilic Parents.

ABSTRACT: Cellulases from glycoside hydrolase family 5 (GH5) are key endoglucanase enzymes in the degradation of diverse polysaccharide substrates and are used in industrial enzyme cocktails to break down biomass. The GH5 family shares a canonical (βα)₈-barrel structure, where each (βα) module is essential for the enzyme's stability and activity. Despite their shared topology, the thermostability of GH5 endoglucanase enzymes can vary significantly, and highly thermostable variants are often sought for industrial applications. Based on the previously characterized thermophilic GH5 endoglucanase Egl5A from Talaromyces emersonii (TeEgl5A), which has an optimal temperature of 90°C, we created 10 hybrid enzymes with elements of the mesophilic endoglucanase Cel5 from Stegonspor

SUBMITTER: Zheng F 

PROVIDER: S-EPMC6384118 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature