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Peptidases specific for proline‐containing peptides and their unusual peptide‐dependent regulation in Oenococcus oeni
Author(s) -
Ritt J.F.,
Remize F.,
Grandvalet C.,
Guzzo J.,
Atlan D.,
Alexandre H.
Publication year - 2009
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1111/j.1365-2672.2008.04032.x
Subject(s) - oenococcus oeni , malolactic fermentation , biochemistry , winemaking , biology , yeast , bacteria , lactic acid , genetics
Aims: Growth of the lactic acid bacterium (LAB) Oenococcus oeni , which is involved in malolactic fermentation during the winemaking process, is stimulated by peptides originating from yeast. In this study, we investigated the impact of peptides on O. oeni growth, peptidase activity and the expression of genes encoding the studied peptidases. Methods and Results: Low levels of PepN activity and very high levels of PepI activity were observed in O. oeni , whereas levels of PepX activity were intermediate. The level of biosynthesis of these O. oeni peptidases was shown to depend on peptides present in the culture medium. These results were confirmed by transcriptional analyses of putative pep genes. The mechanism of repression by peptides did not involve a CodY‐like regulator. Conclusions: Peptides from yeast decrease the levels of enzymatic activity and relative gene expression of O. oeni peptidases. Peptidases specific for proline‐containing peptides are important for O. oeni nitrogen metabolism. Significance and Impact of the Study: We report here for the first time that the enzymes involved in the assimilation of proline‐containing peptides by O. oeni differ from the well‐described proteolytic system of milk LAB. This may reflect a specific adaptation to the wine environment.