Resolution of N‐acetyl‐DL‐methionine methyl ester by the lipase from Brucella thiophenivorans

Abstract

AbstractIn this study, lipase‐catalyzed resolution of N‐acetyl‐DL‐methionine methyl ester (N‐Ac‐DL‐MetOMe) was evaluated. A lipase from Brucella thiophenivorans was prone to exhibit high activity and excellent enantioselectivity toward N‐Ac‐DL‐MetOMe to produce the key chiral intermediate N‐acetyl‐L‐methionine methyl ester (N‐Ac‐L‐MetOMe). The results showed that the enzymatic reaction was carried out in 100 g/L racemic substrate for 2 h, the conversion reached 51.3%, the enantiomeric excess value N‐Ac‐L‐MetOMe exceeded 99%, and the enantiomeric ratio value >200. Therefore, the lipase from B. thiophenivorans has potential prospects for the resolution of N‐Ac‐DL‐MetOMe to produce the important intermediate N‐Ac‐L‐MetOMe.