Purification and characterization of a dipeptidase from Lactobacillus sake

A dipeptidase was purified from cell extracts of Lactobacillus sake. This compound was a monomer having a molecular weight of 50,000 and a pI of 4.7 and exhibited broad specificity against all dipeptides except those with proline or glycine at the N terminus. The enzyme was inhibited by EDTA or 1,10...

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Veröffentlicht in:	Applied and Environmental Microbiology 1995-02, Vol.61 (2), p.837-839
Hauptverfasser:	Montel, M.C. (Institut National de la Recherche Agronomique, Saint-Genes Champanelle, France), Seronie, M.P, Talon, R, Hebraud, M
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino Acid Sequence Analytical, structural and metabolic biochemistry Bacteria Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Chlorides - pharmacology Cobalt - pharmacology CULTIVOS INICIADORES CULTURE STARTER Dipeptidases - antagonists & inhibitors Dipeptidases - chemistry Dipeptidases - isolation & purification Dipeptides - chemistry Ecology, environment Edetic Acid - pharmacology Enzymes Enzymes and enzyme inhibitors Food science Fundamental and applied biological sciences. Psychology Hydrolases Isoelectric Point LACTOBACILLUS Lactobacillus - enzymology Life Sciences Manganese Compounds - pharmacology Meat processing Meat Products - microbiology Mission oriented research Molecular Weight PEPTIDASAS PEPTIDASE PEPTIDE PEPTIDOS Phenanthrolines - pharmacology Physiology and metabolism PURIFICACION PURIFICATION SALCHICHA SAUCISSE Substrate Specificity
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Beschreibung
Zusammenfassung:	A dipeptidase was purified from cell extracts of Lactobacillus sake. This compound was a monomer having a molecular weight of 50,000 and a pI of 4.7 and exhibited broad specificity against all dipeptides except those with proline or glycine at the N terminus. The enzyme was inhibited by EDTA or 1,10-phenanthroline but could be reactivated with CoCl2 and MnCl2
ISSN:	0099-2240 1098-5336
DOI:	10.1128/aem.61.2.837-839.1995