Optical resolution of n-butyl D- and L-lactates using immobilized lipase catalyst

Hitomi Ohara; Masafumi Yamamoto; Akihisa Onogi; Koichi Hirao; Shiro Kobayashi

doi:10.1016/j.jbiosc.2010.08.015

Optical resolution of n-butyl D- and L-lactates using immobilized lipase catalyst

J Biosci Bioeng. 2011 Jan;111(1):19-21. doi: 10.1016/j.jbiosc.2010.08.015. Epub 2010 Sep 18.

Authors

Hitomi Ohara¹, Masafumi Yamamoto, Akihisa Onogi, Koichi Hirao, Shiro Kobayashi

Affiliation

¹ R&D Center for Bio-based Materials, Kyoto Institute of Technology, Matsugasaki Sakyo-ku, Kyoto 606-8585, Japan. ohara@kit.jp

PMID: 20851671
DOI: 10.1016/j.jbiosc.2010.08.015

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%.

MeSH terms

Enzymes, Immobilized / chemistry*
Kinetics
Lactates / chemistry*
Lipase / chemistry*
Magnetic Resonance Spectroscopy
Mass Spectrometry

Substances

Enzymes, Immobilized
Lactates
n-butyl lactate
Lipase