KINETICS OF PEPTIDE AMIDASE AND ITS APPLICATION FOR THE RESOLUTION OFRACEMATES

Authors
STELKESRITTER U BECKERS G BOMMARIUS A DRAUZ K GUNTHER K MOTTENHAHN M SCHWARM M KULA MR
Citation
U. Stelkesritter et al., KINETICS OF PEPTIDE AMIDASE AND ITS APPLICATION FOR THE RESOLUTION OFRACEMATES, Biocatalysis and biotransformation, 15(3), 1997, pp. 205-219
Citations number
16
Categorie Soggetti
Biology,"Biothechnology & Applied Migrobiology
Journal title
Biocatalysis and biotransformation → ACNP
ISSN journal
10242422
Volume
15
Issue
3
Year of publication
1997
Pages
205 - 219
Database
ISI
SICI code
1024-2422(1997)15:3<205:KOPAAI>2.0.ZU;2-4
Abstract
The chemical synthesis of various N-protected amino acid amides was ca rried out. These compounds served as substrates to determine the V-max and K-M values for the deamidation catalyzed by the peptide amidase f rom Citrus sinensis and Stenotrophomonas maltophilia, respectively, an d to investigate the influence of the side chain of the amino acid on the performance of the enzymatic hydrolysis. The enzymatic resolution of racemic N-acetyl amino acids amides yielded N-acetyl-L-amino acids in optical purity greater than or equal to 99% at complete conversion.