title: Optical resolution of n-butyl D- and L-lactates using immobilized lipase catalyst.
abstract: n-Butyl D- and L-lactates (BuDLa and BuLLa) were incubated with immobilized lipase. (1)H-NMR showed that BuDLa reacted to oligomers, while BuLLa did not react. A mixture containing 90.4% of BuLLa and 9.6% of BuDLa was incubated with the enzyme for 72 h, then distilled. The purity of BuLLa increased to 98.6%.
authors.affiliation: R&D Center for Bio-based Materials, Kyoto Institute of Technology, Matsugasaki Sakyo-ku, Kyoto 606-8585, Japan. ohara@kit.jp
authors.forename: Hitomi
authors.initials: H
authors.lastname: Ohara
authors.forename: Masafumi
authors.initials: M
authors.lastname: Yamamoto
authors.forename: Akihisa
authors.initials: A
authors.lastname: Onogi
authors.forename: Koichi
authors.initials: K
authors.lastname: Hirao
authors.forename: Shiro
authors.initials: S
authors.lastname: Kobayashi
mesh_terms: D004800:Enzymes, Immobilized / Q000737:chemistry*; D007700:Kinetics; D007773:Lactates / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry
chemical_list: D004800:Enzymes, Immobilized; D007773:Lactates; C114966:n-butyl lactate; D008049:Lipase