IMMOBILIZED ASPERGILLUS-ORYZAE PROTEASE-CATALYZED FORMATION OF PEPTIDE-BONDS IN ORGANIC-SOLVENT

Citation
Il. Shih et al., IMMOBILIZED ASPERGILLUS-ORYZAE PROTEASE-CATALYZED FORMATION OF PEPTIDE-BONDS IN ORGANIC-SOLVENT, Journal of the Chinese Chemical Society, 44(3), 1997, pp. 327-330
Citations number
21
Categorie Soggetti
Chemistry
ISSN journal
00094536
Volume
44
Issue
3
Year of publication
1997
Pages
327 - 330
Database
ISI
SICI code
0009-4536(1997)44:3<327:IAPFOP>2.0.ZU;2-T
Abstract
Immobilized Aspergillus oryzae protease (AOP) catalyzed the formation of peptide bonds between N-protected amino acids and amino acid eaters or amides in ethyl acetate. The influences of pH and reaction time on the coupling of Boc-L-Tyr and Gly-NH2 were studied. The optimal react ion condition for this enzyme catalyzed synthesis of Boc-L-Phe-Gly-NH2 (98.66%) was at pH 5.5 and a duration of 48 hours.