NOVEL OPTICAL RESOLUTION OF PHENYLALANINE RACEMATE UTILIZING ENZYME REACTION AND MEMBRANE EXTRACTION

Citation
K. Abe et al., NOVEL OPTICAL RESOLUTION OF PHENYLALANINE RACEMATE UTILIZING ENZYME REACTION AND MEMBRANE EXTRACTION, Separation science and technology, 32(11), 1997, pp. 1921-1935
Citations number
22
Categorie Soggetti
Engineering, Chemical",Chemistry
ISSN journal
01496395
Volume
32
Issue
11
Year of publication
1997
Pages
1921 - 1935
Database
ISI
SICI code
0149-6395(1997)32:11<1921:NOROPR>2.0.ZU;2-S
Abstract
A novel optical resolution method for D,L-phenylalanine in which an en zyme reaction and a membrane extraction are combined has been designed . In the first stage only the L-isomer of the racemic phenylalanine me thyl ester was selectively hydrolyzed by the enzyme alpha-chymotrypsin . Further, the unreacted ester was selectively recovered from the mixt ure of the transferred amino acid and the ester form by a membrane ext ractor. Effects of operation conditions in the enzyme reaction and the membrane extraction on the separation efficiency were investigated. T he pH in the material sources is found to be an important factor in th e activity and selectivity for the enzymatic resolution. A novel immob ilized enzyme enables the expensive enzyme to be reused in the feed so lutions. The hollow-fiber membrane extractor was a good separator for an amino acid and its ester derivative, because only the ester was sel ectively extracted into an organic phase. The novel separation system becomes a very useful process for the optical resolution of amino acid s by combining the enzyme reaction with a membrane extraction.