Lignocellulose binding of a Cel5A-RtCBM11 chimera with enhanced β-glucanase activity monitored by electron paramagnetic resonance

Lignocellulose binding of a Cel5A-RtCBM11 chimera with enhanced β-glucanase activity monitored by electron paramagnetic resonance

Abstract Background The Bacillus subtilis endo-β-1,4-glucanase (BsCel5A) hydrolyzes β-1,3-1,4-linked glucan, and the enzyme includes a family 3 carbohydrate-binding module (CBM3) that binds β-1,4-linked glucan. Methods Here we investigate the BsCel5A β-1,3-1,4 glucanase activity after exchanging the...

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Bibliographic Details
Main Authors: Raquel Fonseca-Maldonado, Luana P. Meleiro, Luís F. S. Mendes, Luana F. Alves, Sibeli Carli, Lucas D. Morero, Luis G. M. Basso, Antonio J. Costa-Filho, Richard J. Ward
Format: Article
Language:English
Published: BMC 2017-11-01
Series:Biotechnology for Biofuels
Subjects:
Electron paramagnetic resonance
Site-directed spin labeling
Lignocellulose binding
Enzyme engineering
Online Access:http://link.springer.com/article/10.1186/s13068-017-0964-0

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http://link.springer.com/article/10.1186/s13068-017-0964-0

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