Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

Abstract Background The ascomycete fungus Trichoderma reesei is the predominant source of enzymes for industrial conversion of lignocellulose. Its glycoside hydrolase family 7 cellobiohydrolase (GH7 CBH) TreCel7A constitutes nearly half of the enzyme cocktail by weight and is the major workhorse in...

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Bibliographic Details
Main Authors: Anna S. Borisova, Elena V. Eneyskaya, Suvamay Jana, Silke F. Badino, Jeppe Kari, Antonella Amore, Magnus Karlsson, Henrik Hansson, Mats Sandgren, Michael E. Himmel, Peter Westh, Christina M. Payne, Anna A. Kulminskaya, Jerry Ståhlberg
Format: Article
Language:English
Published: BMC 2018-01-01
Series:Biotechnology for Biofuels
Subjects:
Cellobiohydrolase
Trichoderma atroviride
Trichoderma harzianum
Trichoderma reesei
Cellulase engineering
Online Access:http://link.springer.com/article/10.1186/s13068-017-1006-7

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http://link.springer.com/article/10.1186/s13068-017-1006-7

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