Interfacial molecular interactions of cellobiohydrolase Cel7A and its variants on cellulose.

ABSTRACT: Background:Molecular-scale mechanisms of the enzymatic breakdown of cellulosic biomass into fermentable sugars are still poorly understood, with a need for independent measurements of enzyme kinetic parameters. We measured binding times of cellobiohydrolase Trichoderma reesei Cel7A (Cel7A) on celluloses using wild-type Cel7A (WTintact), the catalytically deficient mutant Cel7A E212Q (E212Qintact) and their proteolytically isolated catalytic domains (CD) (WTcore and E212Qcore, respectively). The binding time distributions were obtained from time-resolved, super-resolution images of fluorescently labeled enzymes on cellulose obtained with total internal reflection fluorescence microscopy. Results:Binding of WTintact and E212Qintact on the recalcitrant algal cellulose (AC) showed two bound populations: ~?85% bound with shorter residence times of

SUBMITTER: Mudinoor AR 

PROVIDER: S-EPMC6969433 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature