Article
Enhancing the thermostability of fumarase C from Corynebacterium glutamicum via molecular modification.
Enzyme and microbial technology - 1 Aug 2018
Lin Ling, Wang Ying, Wu Mianbin, Zhu Li, Yang Lirong, Lin Jianping
Abstract excerpt
Fumarases have been successfully applied in industry for the production of l-malate. However, the industrialization of fumarases is limited by their low thermostability. In this study, the thermostability of fumarase C from Corynebacterium glutamicum was enhanced through directed evolution, simulated mutagenesis, site-directed mutagenesis and saturated mutagenesis. Mutant 2G (A411V) was initially constructed...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Cloning, Molecular
- Corynebacterium glutamicum
- Enzyme Stability
- Fumarate Hydratase
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation