Computational design of α-amylase from Bacillus licheniformis to increase its activity and stability at high temperatures.
作者：
Fan, Shuai;Lü, Xudong;Wei, Xiyu;Lü, Ruijie;Feng, Cuiyue;...
作者机构：
Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100050, China
School of Pharmacy, North China University of Science and Technology, Tangshan 063210, Hebei, China
School of Pharmacy, Jining Medical University, Rizhao 276800, Shandong, China
语种：
英文
关键词：
Molecular dynamics,Protein engineering,Thermostability,amylase
期刊：
Computational and Structural Biotechnology Journal
ISSN：
2001-0370
年：
2024
卷：
23
页码：
982-989
摘要：
The thermostable α-amylase derived from Bacillus licheniformis (BLA) has multiple advantages, including enhancing the mass transfer rate and by reducing microbial contamination in starch hydrolysis. Nonetheless, the application of BLA is constrained by the accessibility and stability of enzymes capable of achieving high conversion rates at elevated temperatures. Moreover, the thermotolerance of BLA requires further enhancement. Here, we developed a computational strategy for constructing small and smart mutant libraries to identify variants with enhanced thermostability. Initially, molecular dynamics (MD) simulations were employed to identify the regions with high flexib...
