Title : Resolution of N-acetyl-DL-methionine methyl ester by the lipase from Brucella thiophenivorans - Li_2024_Chirality_36_e23643 |
Author(s) : Li X , Li Q , Yang L , Huang L , Peng C , Zheng J |
Ref : Chirality , 36 :e23643 , 2024 |
Abstract :
In 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. |
PubMedSearch : Li_2024_Chirality_36_e23643 |
PubMedID: 38384156 |
Substrate | N-Ac-DL-MetOMe |
Li X, Li Q, Yang L, Huang L, Peng C, Zheng J (2024)
Resolution of N-acetyl-DL-methionine methyl ester by the lipase from Brucella thiophenivorans
Chirality
36 :e23643
Li X, Li Q, Yang L, Huang L, Peng C, Zheng J (2024)
Chirality
36 :e23643