122674-97-9Relevant academic research and scientific papers
Enantioselective inhibition: a strategy for improving the enantioselectivity of biocatalytic systems
Guo,Sih
, p. 6836 - 6841 (1989)
Dextromethorphan (DM) and levomethorphan (LM) were found to be effective enantioselective inhibitors of Candida cylindracea lipase-catalyzed hydrolysis of a variety of (±)-arlypropionic and (±)-(arloxy)propionic esters. The enantioselectivity of the biocatalytic resolution of (±)-methyl 2-(2,4-dichlorophenoxy)propionate (DCPP) was enhanced 20-fold in the presence of either DM or LM. A general model for enantioselective inhibition has been developed, and a quantitative expression has been derived to show the underlying parameters that govern enantioselective inhibition. To define the mechanism of action of DM, a series of kinetic inhibition experiments was conducted with enantiomerically pure (R)-(+)-DCPP and (S)-(-)-DCPP. The observed inhibition pattern was that of partial noncompetitive inhibition for (R)-(+)-DCPP and that of pure noncompetitive inhibition for (S)-(-)-DCPP.
Enhancement of the enantioselectivity of lipase OF catalyzed hydrolysis
Chang, Yuan-Fung,Tai, Dar-Fu
, p. 177 - 179 (2001)
By rational purification of lipase OF on a mercurial affinity column three fractions were identified as responsible for the improved enantioselectivity without compromising the total activity of the crude enzyme. These three portions of lipase OF have remarkably different abilities to differentiate between the enantiomers of α-arylpropionic acids in the lipase catalyzed hydrolysis of the corresponding esters.
