Optical resolution of various amino acids using a supported liquid membrane encapsulating a surfactant-protease complex

Eijiro Miyako, Tatsuo Maruyama, Fukiko Kubota, Noriho Kamiya, Masahiro Goto

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

We have encapsulated a surfactant-protease complex (the main protease used being a-chymotrypsin) in an organic phase of a supported liquid membrane (SLM) for the optical resolution of various amino acids. L-Isomers of amino acids were enantioselectively permeated through the SLM. The mechanism of the amino acid permeation through the SLM was considered to be as follows; an L-amino acid was enantioselectively esterified with ethanol by a surfactant-protease complex encapsulated in the SLM, and the resulting L-amino acid ethyl ester dissolved into the organic phase of the SLM and diffused across the SLM. Another surfactant-α-chymotrypsin complex in the receiving phase catalyzed ester hydrolysis to produce the initial L-amino acid and ethanol, which are water-soluble. Thus, the L-amino acid was selectively transported to the receiving phase through the SLM on the basis of the molecular recognition of the surfactant-protease complex in the SLM. It was found that the catalytic activity and enantioselectivity of the surfactant-protease complex governed the permeate flux of amino acids and the enantiomeric excess in the membrane separation.

Original languageEnglish
Pages (from-to)4674-4679
Number of pages6
JournalLangmuir
Volume21
Issue number10
DOIs
Publication statusPublished - May 10 2005

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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