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 (WT_intact), the catalytically deficient mutant Cel7A E212Q (E212Q_intact) and their proteolytically isolated catalytic domains (CD) (WT_core and E212Q_core, 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 WT_intact

SUBMITTER: Mudinoor AR 

PROVIDER: S-EPMC6969433 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature