Abstract
To further improve the activity and enantioconvergency of PvEH3G170E for racemic (rac-) p-chlorostyrene oxide (pCSO), its F187 was randomly substituted by saturation mutagenesis. The double-site variants of pveh3, pET-28a-pveh3G170E/F187X (X: any one of 20 residues), were transformed into E. coli BL21(DE3), thereby constructing a mutagenesis library (E. coli/pveh3G170E/F187X). E. coli/pveh3G170E/F187L had the highest EH activity of 19.64 U/g wet cell, while /pveh3G170E/F187I the highest αS of 94.5%. The enantioconvergent hydrolysis of 150 mM rac-pCSO by E. coli/pveh3G170E/F187I produced (R)-p-chlorophenyl-1,2-ethanediol with 92.8% eep and 8.68 mmol/h/L space-time yield. The mechanism of PvEH3G170E/F187I with improved enantioconvergency was analyzed by molecular docking simulation.
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