Improvement of thermostability and catalytic efficiency of glucoamylase from Talaromyces leycettanus JCM12802 via site-directed mutagenesis to enhance industrial saccharification applications

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...

Full description

Bibliographic Details
Main Authors: Bai, Y. (Author), Huang, H. (Author), Luo, H. (Author), Qin, X. (Author), Tong, L. (Author), Tu, T. (Author), Wang, X. (Author), Wang, Y. (Author), Yang, H. (Author), Yao, B. (Author), Zheng, J. (Author)
Format: Article
Language:English
Published: BioMed Central Ltd 2021
Subjects:
catalysis
catalyst
Catalyst activity
Catalytic efficiencies
Catalytic efficiency
Cloning
Covalent bonds
Efficiency
Efficiency limits
efficiency measurement
Encoding genes
enzyme
Enzyme activity
fungus
Gene encoding
Glucoamylase
Industrial application
Industrial enzymes
Molecular dynamics
Mutagenesis
mutagenicity
Optimal temperature
Pichia pastoris
Property
reaction kinetics
Saccharification
Site directed mutagenesis
Site-directed mutagenesis
Stability
stability analysis
Starch
Starch industry
Sulfur compounds
Talaromyces leycettanus
thermal structure
Thermophilic fungus
Thermostability
Online Access:View Fulltext in Publisher

Internet

View Fulltext in Publisher

Similar Items