Significantly improved thermostability of a reductase CgKR1 from Candida glabrata with a key mutation at Asp 138 for enhancing bioreduction of aromatic α-keto esters.

Abstract excerpt

The keto ester reductase from Candida glabrata, designated as CgKR1, is a highly versatile biocatalyst with a broad substrate spectrum. Its substrate preference was altered by rational design of the active pocket for bioreduction of aromatic α-keto esters in our previous work. However, its practical application is still hindered by its poor thermostability and high biocatalyst loading. In this work, random...

Topics

• Amino Acid Substitution
• Candida glabrata
• Enzyme Stability
• Escherichia coli
• Esters
• Fungal Proteins
• Hot Temperature
• Mutagenesis, Site-Directed
• Mutation
• Oxidation-Reduction
• Oxidoreductases