PURIFICATION AND CHARACTERIZATION OF AN L-AMINOPEPTIDASE FROM PSEUDOMONAS-PUTIDA ATCC 12633

Citation
Hfm. Hermes et al., PURIFICATION AND CHARACTERIZATION OF AN L-AMINOPEPTIDASE FROM PSEUDOMONAS-PUTIDA ATCC 12633, Applied and environmental microbiology, 59(12), 1993, pp. 4330-4334
Citations number
16
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
ISSN journal
00992240
Volume
59
Issue
12
Year of publication
1993
Pages
4330 - 4334
Database
ISI
SICI code
0099-2240(1993)59:12<4330:PACOAL>2.0.ZU;2-R
Abstract
An L-aminopeptidase of Pseudomonas putida, used in an industrial proce ss for the hydrolysis Of D,L-amino acid amide racemates, was purified to homogeneity. The highly L-enantioselective enzyme resembled thiol r eagent-sensitive alkaline serine proteinases and was strongly activate d by divalent cations. It possessed a high substrate specificity for d ipeptides and alpha-H amino acid amides, e.g., L-phenylglycine amide.