Interfacial molecular interactions of cellobiohydrolase Cel7A and its variants on cellulose

Autor:	Akshata R. Mudinoor, Peter M. Goodwin, Raghavendra U. Rao, Nardrapee Karuna, Alex Hitomi, Jennifer Nill, Tina Jeoh
Jazyk:	angličtina
Rok vydání:	2020
Předmět:	Trichoderma reesei Cel7A Super-resolution Single-molecule imaging Catalytic domain Binding lifetime Dissociation rate Fuel TP315-360 Biotechnology TP248.13-248.65
Zdroj:	Biotechnology for Biofuels, Vol 13, Iss 1, Pp 1-16 (2020)
Druh dokumentu:	article
ISSN:	1754-6834
DOI:	10.1186/s13068-020-1649-7
Popis:	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
Databáze:	Directory of Open Access Journals
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