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Issue Lait
Volume 75, Number 4-5, 1995
1st International Symposium on Propionibacteria.
Page(s) 325 - 330
DOI http://dx.doi.org/10.1051/lait:19954-524

Lait 75 (1995) 325-330
DOI: 10.1051/lait:19954-524

Protein degradation and amino acid metabolism by propionibacteria

T. Langsrud, T. Sorhaug and G.E. Vegarud

Department of Food Science, The Agricultural University of Norway, 1432 Aas, Norway

Abstract - This article reports the existing knowledge about the proteolytic system of Propionibacterium and its ability to degrade amino acids. Propionibacterium contains at least 2 weak proteinases, 1 cell wall-associated and 1 intracellular or membrane-bound. A wide variety of peptidases, such as amino peptidases, proline iminopeptidase, proline imidopeptidase, X-prolyl-dipeptidyl-amino-peptidase, endopeptidases and carboxypeptidase, has been described and characterized. A wide variety of amino acids, especially aspartic acid, alanine, serine and glycine, were easily degraded by Propionibacterium, but large strain and species variations were observed.


Résumé - Dégradation protéique et métabolisme des acides aminés par les bactéries propioniques
Cet article fait l'état des connaissances actuelles sur le système protéolytique des bactéries propioniques, et sur sa capacité à dégrader des acides aminés. Propionibacterium contient au moins deux protéinases, l'une associée à la paroi cellulaire et l'autre cytoplasmique ou membranaire. Une vaste variété de peptidases ont été décrites et caractérisées, telles que aminopeptidases, proline iminopeptidase, proline imidopeptidase, X-prolyl-dipeptidyl-aminopeptidase, endopeptidases et carboxypeptidase. Une grande variété d'acides aminés, en particulier l'acide aspartique, l'alanine, la sérine et la glycine, pouvaient être facilement dégradés par Propionibacterium, mais de grandes variations dues à la souche et à l'espèce étudiée ont été observées.


Key words: Propionibacterium / proteinase / peptidase / amino acid

Mots clés : Propionibacterium / protéinase / peptidase / acide aminé




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