Article
Effect of the single mutation N9Y on the catalytical properties of xylanase Xyn11A from Cellulomonas uda: a biochemical and molecular dynamic simulation analysis.
Bioscience, biotechnology, and biochemistry - 25 Aug 2021
Cayetano-Cruz Maribel, Caro-Gómez Luis A, Plascencia-Espinosa Miguel, Santiago-Hernández Alejandro, Benítez-Cardoza Claudia G, Campos Jorge E, Hidalgo-Lara María Eugenia, Zamorano-Carrillo Absalom
Abstract excerpt
Cellulomonas uda produces Xyn11A, moderately thermostable xylanase, with optimal activity at 50 °C and pH 6.5. An improvement in the biochemical properties of Xyn11A was achieved by site-directed mutagenesis approach. Wild-type xylanase, Xyn11A-WT, and its mutant Xyn11A-N9Y were expressed in Escherichia coli, and then both enzymes were purified and characterized. Xyn11A-N9Y displayed optimal activity at 60 °C and...
Topics
- Amino Acid Sequence
- Catalysis
- Cellulomonas
- Endo-1,4-beta Xylanases
- Escherichia coli
- Molecular Dynamics Simulation
- Mutation
- Protein Conformation