Article
Mutagenesis for Improvement of Activity and Stability of Prolyl Aminopeptidase from Aspergillus oryzae.
Applied biochemistry and biotechnology - 1 Aug 2020
Liu Dehua, Zhang Dawei, Huang Qinqin, Gu Lili, Zhou Nandi, Tian Yaping
Abstract excerpt
In this study, the prokaryotic expression system of Escherichia coli was used to modify prolyl aminopeptidase derived from Aspergillus oryzae JN-412 (AoPAP) via random mutagenesis and site-directed saturation mutagenesis. A random mutant library with a capacity of approximately 3000 mutants was compiled using error-prone polymerase chain reaction, and nonconservative amino acids within 3 Å of the substrate...
Topics
- Aminopeptidases
- Aspergillus oryzae
- Enzyme Stability
- Escherichia coli
- Hydrogen-Ion Concentration
- Industrial Microbiology
- Kinetics
- Molecular Docking Simulation
- Mutagenesis
- Mutagenesis, Site-Directed