title: Enhancing the enantioselectivity of lipase in transesterification by substrate matching: an enzyme memory based approach.
abstract: The substrate matching strategy is described as a new approach for effectively enhancing the lipase enantioselectivity in organic solvent. In the lipase-catalyzed transesterifications of 3a-c, higher enantioselectivities have been achieved using 1a-c, respectively, as the structurally matched acyl donors.
authors.affiliation: Department of Chemistry, Division of Molecular and Life Science, Pohang University of Science and Technology, San 31 Hyojadong, Pohang, Kyungbuk 790-784, Korea.
authors.forename: D
authors.initials: D
authors.lastname: Lee
authors.forename: Y K
authors.initials: YK
authors.lastname: Choi
authors.forename: M J
authors.initials: MJ
authors.lastname: Kim
mesh_terms: D016956:Burkholderia cepacia / Q000201:enzymology; D002175:Candida / Q000201:enzymology; D004952:Esters / Q000737:chemistry*; D008049:Lipase / Q000378:metabolism; D012997:Solvents; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D004952:Esters; D012997:Solvents; D008049:Lipase