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Kinetic Resolution of Racemic α‐Methyl‐β‐propiothiolactone by Lipase‐Catalyzed Hydrolysis
Author(s) -
Hwang BumYeol,
Lee Hee Bong,
Kim Young Gyu,
Kim ByungGee
Publication year - 2000
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp000120a
Subject(s) - chemistry , hydrolysis , lipase , substrate (aquarium) , kinetic resolution , catalysis , product inhibition , cyclohexane , titration , triacylglycerol lipase , solvent , organic chemistry , medicinal chemistry , enzyme , enantioselective synthesis , non competitive inhibition , oceanography , geology
Kinetic resolution of racemic α‐methyl‐β‐propiothiolactone ( rac ‐MPTL) using lipases in organic solvent was studied. The lipase from Pseudomonas cepacia (PCL) showed the highest ( S )‐enantioselectivity ( E > 100), and cyclohexane containing 1% (v/v) buffer was identified as the best reaction medium for maintaining high enantioselectivity as well as high reaction rate. While the substrate inhibition was not observed up to 300 mM rac ‐MPTL, severe product inhibition was observed even at 50 mM racemic 3‐mercapto‐α‐methyl propionic acid ( rac ‐MMPA), which made the use of high substrate concentration difficult. To overcome the product inhibition, the products, ( R )‐MMPA, were neutralized by addition of a dilute basic solution. Although the resolution reaction proceeded further by the base titration, the enantioselectivity of the reaction decreased as a result of nonenantioselective hydrolysis of rac ‐MPTL in the basic solution. Under these conditions, 200 mM rac ‐MPTL was successfully resolved to above 95% ee S with 53% conversion.