Mutations in the substrate entrance region of -glucosidase from Trichoderma reesei improve enzyme activity and thermostability-Reference-Cited by-同舟云学术

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Mutations in the substrate entrance region of -glucosidase from Trichoderma reesei improve enzyme activity and thermostability

Published:2012-10-16 Issue:11 Volume:25 Page:733-740
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering Design and Selection

Author:

Lee H.-L.,Chang C.-K.,Jeng W.-Y.,Wang A. H.- J.,Liang P.-H.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/25/11/733/4372578/gzs073.pdf

Reference34 articles.

1. Increased Thermal Resistance and Modification of the Catalytic Properties of a β-Glucosidase by Random Mutagenesis andin Vitro Recombination

2. Cloning and Characterization of Two β-Glucosidase/Xylosidase Enzymes from Yak Rumen Metagenome

3. Biosynthetic Activity of Recombinant Escherichia coli-Expressed Pichia etchellsii β-Glucosidase II

4. Ethanol Production from Agricultural Biomass Substrates

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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3. Structural analysis of tris binding in β-glucosidases;Biochemical and Biophysical Research Communications;2024-01

4. Improving the cellobiose hydrolysis activity of glucose-stimulating β-glucosidase Bgl2A;Enzyme and Microbial Technology;2023-09

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