Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties

Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties

Abstract Background The non-productive adsorption of cellulases onto lignin in biomass is a key issue for the biofuel process economy. It would be helpful to reduce the inhibitory effect of lignin on enzymatic hydrolysis by engineering weak lignin-binding cellulases. Cellulase linkers are highly div...

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Bibliographic Details
Main Authors: Zhen Wang, Tianrui Zhang, Liangkun Long, Shaojun Ding
Format: Article
Language:English
Published: BMC 2018-12-01
Series:Biotechnology for Biofuels
Subjects:
GH5 endoglucanase
Processive enzyme
Lignin binding
Polypeptide linker
Quartz crystal microgravimetry
Online Access:http://link.springer.com/article/10.1186/s13068-018-1333-3

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http://link.springer.com/article/10.1186/s13068-018-1333-3

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