There is an "I" in team: individual improvements in supercharged cellulase cocktail facilitates cooperative cellulose degradation.

ABSTRACT: Lignocellulosic biomass is an abundant renewable carbon source for biofuel production, but its conversion to fermentable sugars is hindered by poor cellulase activity on highly crystalline and insoluble cellulose. While pretreatment makes biomass more amenable to enzymatic degradation, several issues linger related to productive enzyme binding and efficient catalytic turnover. To address this bottleneck, we employed protein supercharging to rationally design a glycosyl hydrolase (GH) family-6 exocellulase (Cel6B) and its native family-2a carbohydrate binding module (CBM2a) from the thermophilic cellulolytic microbe Thermobifida fusca. A chimeric library of 32 supercharged constructs rationally designed across both GH/CBM domains was synthesized and expressed in E. coli. Screening of the en

SUBMITTER: DeChellis A 

PROVIDER: S-EPMC12874829 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature