Article
Engineering of the Phytase YiAPPA to Improve Thermostability and Activity and Its Application Potential in Dephytinization of Food Ingredients.
Journal of microbiology and biotechnology - 28 Aug 2024
Zeng Jing, Guo Jianjun, Yuan Lin
Abstract excerpt
The aim of this study was to modify phytase YiAPPA via protein surficial residue mutation to obtain phytase mutants with improved thermostability and activity, enhancing its application potential in the food industry. First, homology modeling of YiAPPA was performed. By adopting the strategy of p...
Topics
- 6-Phytase
- Enzyme Stability
- Mutagenesis, Site-Directed
- Molecular Dynamics Simulation
- Protein Engineering
- Hydrogen-Ion Concentration
- Kinetics
- Phytic Acid
- Models, Molecular
- Temperature
- Hot Temperature
- Mutation
- Escherichia coli
- Food Industry
- Acid Phosphatase
- Escherichia coli Proteins