RESOLUTION OF NONPROTEIN AMINO-ACIDS VIA MICROBIAL PROTEASE-CATALYZEDESTER HYDROLYSIS - MARKED ENHANCEMENT OF ENANTIOSELECTIVITY BY THE USE OF ESTERS WITH LONGER ALKYL CHAINS AND AT LOW-TEMPERATURE

Authors
MIYAZAWA T MINOWA H MIYAMOTO T IMAGAWA K YANAGIHARA R YAMADA T
Citation
T. Miyazawa et al., RESOLUTION OF NONPROTEIN AMINO-ACIDS VIA MICROBIAL PROTEASE-CATALYZEDESTER HYDROLYSIS - MARKED ENHANCEMENT OF ENANTIOSELECTIVITY BY THE USE OF ESTERS WITH LONGER ALKYL CHAINS AND AT LOW-TEMPERATURE, Tetrahedron : asymmetry, 8(3), 1997, pp. 367-370
Citations number
19
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Inorganic & Nuclear","Chemistry Physical
Journal title
Tetrahedron : asymmetry → ACNP
ISSN journal
09574166
Volume
8
Issue
3
Year of publication
1997
Pages
367 - 370
Database
ISI
SICI code
0957-4166(1997)8:3<367:RONAVM>2.0.ZU;2-4
Abstract
In the microbial protease-catalyzed hydrolysis of amino acid esters wi th the free alpha-amino group, the enantioselectivity can be enhanced greatly by employing esters with longer alkyl chains such as the isobu tyl ester instead of the conventional methyl ester and by conducting t he reaction at low temperature. (C) 1997 Elsevier Science Ltd. All rig hts reserved.