A single site mutation significantly improves the thermostability and activity of heparinase I from Bacteroides eggerthii
Author:
Affiliation:
1. School of Pharmacy, Jiangsu University, Zhenjiang, People’s Republic of China
2. College of Petroleum and Chemical Engineering, Beibu Gulf University, People’s Republic of China
Funder
Natural Science Foundation of Guangxi Province
National Natural Science Foundation of China
Publisher
Informa UK Limited
Subject
Biochemistry,Catalysis,Biotechnology
Link
https://www.tandfonline.com/doi/pdf/10.1080/10242422.2021.1976757
Reference29 articles.
1. Approaching boiling point stability of an alcohol dehydrogenase through computationally-guided enzyme engineering
2. Ultrasonic-assisted preparation of a low molecular weight heparin (LMWH) with anticoagulant activity
3. Protein engineering for unusual environments
4. GROMACS: A message-passing parallel molecular dynamics implementation
5. Purification and characterization of a novel heparinase.
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