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Relationships between arginine degradation, pH and survival in Lactobacillus sakei
Author(s) -
Champomier Vergès MarieChristine,
Zuñiga Manuel,
MorelDeville Françoise,
PérezMartínez Gaspar,
Zagorec Monique,
Ehrlich S.Dusko
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb08809.x
Subject(s) - arginine deiminase , arginine , biochemistry , catabolite repression , lactobacillus sakei , biology , ornithine carbamoyltransferase , fermentation , chemistry , mutant , ornithine , microbiology and biotechnology , lactobacillus , amino acid , gene
Lactobacillus sakei is one of the most important lactic acid bacteria of meat and fermented meat products. It is able to degrade arginine with ammonia and ATP production by the arginine deiminase pathway (ADI). This pathway is composed of three enzymes: arginine deiminase, ornithine transcarbamoylase and carbamate kinase, and an arginine transport system. The transcription of the ADI pathway is induced by arginine and subjected to catabolite repression. In order to understand the physiological role of the degradation of this amino acid we investigated the growth of bacteria under various conditions. We show that arginine degradation is responsible for an enhanced viability during the stationary phase when cells are grown under anaerobiosis. Arginine is necessary for the induction of the ADI pathway but in association with another environmental signal. Using a mutant of the L ‐lactate dehydrogenase unable to lower the pH we could clearly demonstrate that (i) low pH is not responsible for cell death during the stationary phase, so survival is due to another factor than elevated pH, (ii) neither low pH nor oxygen limitation is responsible for the induction of the ADI pathway together with arginine since the ldhL mutant is able to degrade arginine under aerobiosis.

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