Article
Conserved cysteine variants of metagenomic derived polygalacturonase concurrently shift its optima at acidic pH and enhanced thermostability: structural and functional analysis.
Journal of biomolecular structure & dynamics - 1 Jan 2019
Singh Rajvinder, Kumar Arbind, Chopra Nisha, Mahajan Ritu, Kaur Jagdeep
Abstract excerpt
To study the effect of conserved cysteins on biochemical properties of a previously cloned metagenomic polygalacturonase (PecJKR01), single point variants A42C, M283C, and double variants M283C + F24C, M283C + A42C were constructed. Mutations resulted in shifting the pH toward lower range and enhanced thermostability. The mutants were optimally active at pH 5.0 as compared to pH 7.0 for wild type. Point variants...
Topics
- Cysteine
- Enzyme Stability
- Hydrogen-Ion Concentration
- Kinetics
- Metagenomics
- Models, Molecular
- Mutation
- Polygalacturonase
- Structure-Activity Relationship
- Temperature
