Article
Enhancing the thermostability of a cold-active lipase from Penicillium cyclopium by in silico design of a disulfide bridge.
Applied biochemistry and biotechnology - 1 Aug 2014
Tan Zhongbiao, Li Jianfang, Wu Minchen, Wang Junqing
Abstract excerpt
Cysteine mutants of a cold-active lipase (PcLipI) from Penicillium cyclopium were designed by the software Disulfide by Design Ver. 1.20 in an effort to improve enzyme thermostability by addition of a disulfide bridge. Those mutants predicted by molecular dynamics simulation to have better thermo...
Topics
- Cold Temperature
- Computer Simulation
- Disulfides
- Enzyme Stability
- Escherichia coli
- Lipase
- Models, Molecular
- Mutation
- Penicillium
- Pichia
- Protein Conformation
- Protein Engineering
- Recombinant Proteins
- Software