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Appl Environ Microbiol, April 1998, p. 1230-1236, Vol. 64, No. 4
Unité de Recherches Laitières et
Génétique Appliquée1 and
Unité de Biochimie et Structure des
Protéines,2 Institut National de la
Recherche Agronomique, Centre de Recherches de Jouy-en-Josas, 78350 Jouy-en-Josas, France
Received 16 September 1997/Accepted 29 January 1998
To study the substrate specificity of the oligopeptide transport
system of Lactococcus lactis for its natural substrates, the growth of L. lactis MG1363 was studied in a chemically
defined medium containing milk peptides or a tryptic digest of
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Specificity of Milk Peptide Utilization by
Lactococcus lactis
s2-casein as the source of amino acids. Peptides were
separated into acidic, neutral, and basic pools by solid-phase
extraction or by cation-exchange liquid chromatography. Their ability
to sustain growth and the time course of their utilization demonstrated
the preferential use of hydrophobic basic peptides with molecular
masses ranging between 600 and 1,100 Da by L. lactis MG1363
and the inability to use large, acidic peptides. These peptide
utilization preferences reflect the substrate specificity of the
oligopeptide transport system of the strain, since no significant cell
lysis was inferred. Considering the free amino acid content of milk and
these findings on peptide utilization, it was demonstrated that the
cessation of growth of L. lactis MG1363 in milk was due to
deprivation of leucine and methionine.
*
Corresponding author. Mailing address: Unité de
Recherches Laitières et Génétique Appliquée,
Institut National de la Recherche Agronomique, Centre de Recherches de
Jouy-en-Josas, 78350 Jouy-en-Josas, France. Phone: (33) 134 652 068. Fax: (33) 134 652 065. E-mail: juillard{at}jouy.inra.fr.
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