Title : Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols - Wagner_2024_Chembiochem__e202400082 |
Author(s) : Wagner K , Hummel A , Yang J , Horino S , Kanomata K , Akai S , Groger H |
Ref : Chembiochem , :e202400082 , 2024 |
Abstract :
Chiral tertiary alcohols are important organic compounds in science as well as in industry. However, their preparation in enantiomerically pure form is still a challenge due to their complex structure and steric hindrances compared with primary and secondary alcohols, so kinetic resolution could be an attractive approach. Lipase A from Candida antarctica (CAL-A) has been shown to catalyze the enantioselective esterification of various tertiary alcohols with excellent enantioselectivity but low activity. Here we report a mutagenesis study by rational design to improve CAL-A activity against tertiary alcohols. Single mutants of CAL-A were selected, expressed, immobilized and screened for esterification of the tertiary alcohol 1,2,3,4-tetrahydronaphthalene-1-ol. A double mutant V278S+S429G showed a 1.5-fold higher reaction rate than that of the wild type CAL-A, while maintaining excellent enantioselectivity. |
PubMedSearch : Wagner_2024_Chembiochem__e202400082 |
PubMedID: 38670922 |
Wagner K, Hummel A, Yang J, Horino S, Kanomata K, Akai S, Groger H (2024)
Protein engineering of lipase A from Candida antarctica to improve esterification of tertiary alcohols
Chembiochem
:e202400082
Wagner K, Hummel A, Yang J, Horino S, Kanomata K, Akai S, Groger H (2024)
Chembiochem
:e202400082