Cargando…
Improvement of thermostability and catalytic efficiency of glucoamylase from Talaromyces leycettanus JCM12802 via site-directed mutagenesis to enhance industrial saccharification applications
BACKGROUND: Glucoamylase is an important industrial enzyme in the saccharification of starch into glucose. However, its poor thermostability and low catalytic efficiency limit its industrial saccharification applications. Therefore, improving these properties of glucoamylase is of great significance...
Autores principales: | Tong, Lige, Zheng, Jie, Wang, Xiao, Wang, Xiaolu, Huang, Huoqing, Yang, Haomeng, Tu, Tao, Wang, Yuan, Bai, Yingguo, Yao, Bin, Luo, Huiying, Qin, Xing |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8520190/ https://www.ncbi.nlm.nih.gov/pubmed/34656167 http://dx.doi.org/10.1186/s13068-021-02052-3 |
Ejemplares similares
-
Characterization of two thermophilic cellulases from Talaromyces leycettanus JCM12802 and their synergistic action on cellulose hydrolysis
por: Gu, Yuan, et al.
Publicado: (2019) -
Improvement of the thermostability and catalytic efficiency of a highly active β-glucanase from Talaromyces leycettanus JCM12802 by optimizing residual charge–charge interactions
por: You, Shuai, et al.
Publicado: (2016) -
Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A from Talaromyces leycettanus JCM12802 by Rational Design
por: Xia, Wei, et al.
Publicado: (2021) -
A Swollenin From Talaromyces leycettanus JCM12802 Enhances Cellulase Hydrolysis Toward Various Substrates
por: Zhang, Honghai, et al.
Publicado: (2021) -
A GH51 α-l-arabinofuranosidase from Talaromyces leycettanus strain JCM12802 that selectively drives synergistic lignocellulose hydrolysis
por: Tu, Tao, et al.
Publicado: (2019)