Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability
Abstract Endoglucanases are increasingly applied in agricultural and industrial applications as a key biocatalyst for cellulose biodegradation. However, the low performance in extreme conditions seriously challenges the enzyme’s commercial utilization. To obtain endoglucanases with substantially imp...
Guardado en:
Autores principales: | Xiutao Chen, Weiguang Li, Peng Ji, Yang Zhao, Chengyao Hua, Chao Han |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/1fbef55c5f7848819f325ba76a9c1345 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins.
por: Satoshi Akanuma, et al.
Publicado: (2021) -
Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins
por: Satoshi Akanuma, et al.
Publicado: (2021) -
An Engineered Thermostable Laccase with Great Ability to Decolorize and Detoxify Malachite Green
por: Guotao Mao, et al.
Publicado: (2021) -
Thermostable exoshells fold and stabilize recombinant proteins
por: Siddharth Deshpande, et al.
Publicado: (2017) -
A thermostable β-glucuronidase obtained by directed evolution as a reporter gene in transgenic plants.
por: Ai-Sheng Xiong, et al.
Publicado: (2011)