Improved thermostability of a metagenomic glucose-tolerant β-glycosidase based on its X-ray crystal structure
Volume: 101, Issue: 23-24, Pages: 8353 - 8363
Published: Oct 23, 2017
Abstract
MeBglD2, a metagenomic β-glycosidase, is stimulated by various saccharides, including D-glucose, D-xylose, and maltose, and it promotes the enzymatic saccharification of plant biomass. To improve the thermostability of MeBglD2, its X-ray crystal structure was analyzed, and the amino acid residues responsible for its thermostability were identified using the structural information. Mutations in His8, Asn59, and Gly295 improved the thermostability...
Paper Details
Title
Improved thermostability of a metagenomic glucose-tolerant β-glycosidase based on its X-ray crystal structure
Published Date
Oct 23, 2017
Volume
101
Issue
23-24
Pages
8353 - 8363
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