Novel Optical Resolution of Phenylalanine Racemate Utilizing Enzyme Reaction and Membrane Extraction

Kojiro Abe, Masahiro Goto, Fumiyuki Nakashio

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A novel optical resolution method for D,L-phenylalanine in which an enzyme reaction and a membrane extraction are combined has been designed. In the first stage only the L-isomer of the racemic phenylalanine methyl ester was selectively hydrolyzed by the enzyme α-chymotrypsin. Further, the unreacted ester was selectively recovered from the mixture of the transferred amino acid and the ester form by a membrane extractor. Effects of operation conditions in the enzyme reaction and the membrane extraction on the separation efficiency were investigated. The pH in the material sources is found to be an important factor in the activity and selectivity for the enzymatic resolution. A novel immobilized enzyme enables the expensive enzyme to be reused in the feed solutions. The hollow-fiber membrane extractor was a good separator for an amino acid and its ester derivative, because only the ester was selectively extracted into an organic phase. The novel separation system becomes a very useful process for the optical resolution of amino acids by combining the enzyme reaction with a membrane extraction.

Original languageEnglish
Pages (from-to)1921-1935
Number of pages15
JournalSeparation Science and Technology
Volume32
Issue number11
DOIs
Publication statusPublished - Jan 1 1997

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Phenylalanine
Enzymes
Esters
Membranes
Amino acids
Amino Acids
Immobilized Enzymes
Chymotrypsin
Separators
Isomers
Derivatives
Fibers

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)
  • Process Chemistry and Technology
  • Filtration and Separation

Cite this

Novel Optical Resolution of Phenylalanine Racemate Utilizing Enzyme Reaction and Membrane Extraction. / Abe, Kojiro; Goto, Masahiro; Nakashio, Fumiyuki.

In: Separation Science and Technology, Vol. 32, No. 11, 01.01.1997, p. 1921-1935.

Research output: Contribution to journalArticle

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