The ability of Clostridium butyricum cultures in synthetic medium to hydrol
yse the tripeptide Leu-Val-Leu was demonstrated using gas chromatography co
upled with mass spectrometry. Electrospray mass spectrometry was used to co
nfirm this unknown activity for this C-heterotrophic species listed sacchar
olytic, non-proteolytic clostridia. The oligopeptide hydrolysis activity is
characterised by the detection of the released amino acids and the product
s of their bioconversion, the corresponding 2-hydroxyacids. This observatio
n opens new aspects in the study of C. butyricum and raised questions about
the peptide metabolism by this species. The enzymes implied in the oligope
pitide hydrolysis can be regarded as potential virulence factors and being
an element in the comprehension of certain pathologies.
(C) 1999 Academic Press.