Removal of N-linked glycans in cellobiohydrolase Cel7A from Trichoderma reesei reveals higher activity and binding affinity on crystalline cellulose

Removal of N-linked glycans in cellobiohydrolase Cel7A from Trichoderma reesei reveals higher activity and binding affinity on crystalline cellulose

Abstract Background Cellobiohydrolase from glycoside hydrolase family 7 is a major component of commercial enzymatic mixtures for lignocellulosic biomass degradation. For many years, Trichoderma reesei Cel7A (TrCel7A) has served as a model to understand structure–function relationships of processive...

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Bibliographic Details
Main Authors: Bartłomiej M. Kołaczkowski, Kay S. Schaller, Trine Holst Sørensen, Günther H. J. Peters, Kenneth Jensen, Kristian B. R. M. Krogh, Peter Westh
Format: Article
Language:English
Published: BMC 2020-08-01
Series:Biotechnology for Biofuels
Subjects:
GH7 cellulase
Trichoderma reesei Cel7A
Aspergillus oryzae
N-Glycosylation
Heterogeneous interfacial enzyme kinetics
MD
Online Access:http://link.springer.com/article/10.1186/s13068-020-01779-9

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http://link.springer.com/article/10.1186/s13068-020-01779-9

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