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Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
Published on: November 16, 2016
Oligopeptide assimilation and transport by Oenococcus oeni
J-F Ritt1, M Guilloux-Benatier, J Guzzo
1Laboratoire Recherche En Vigne et Vin, Université de Bourgogne, Dijon, France.
Journal of Applied Microbiology
|October 12, 2007
Summary
Oenococcus oeni utilizes oligopeptides as a nitrogen source, transporting and hydrolyzing peptides of two to five amino acids. This finding impacts understanding wine nitrogen composition and O. oeni
Area of Science:
- Microbiology
- Food Science
- Biochemistry
Background:
- Oenococcus oeni is a crucial wine bacterium known for slow growth and low yield.
- This microorganism exhibits a preference for complex nitrogen sources over free amino acids.
- Understanding its nitrogen assimilation is key to optimizing wine fermentation.
Purpose of the Study:
- To investigate the capability of Oenococcus oeni to utilize oligopeptides for growth.
- To characterize the transport and hydrolysis mechanisms of oligopeptides by O. oeni.
Main Methods:
- Assessed the utilization of various oligopeptides (2-8 amino acid residues) by whole O. oeni cells.
- Monitored the disappearance of peptides from the extracellular medium.
- Quantified the release of free amino acids into the medium.
Main Results:
- Oenococcus oeni demonstrated the ability to use several oligopeptides as sources of essential amino acids.
- Peptide utilization rates varied, with concomitant release of free amino acids observed.
- The bacterium successfully transported and hydrolyzed oligopeptides containing two to five amino acid residues.
Conclusions:
- Oenococcus oeni possesses a functional oligopeptide transport and hydrolysis system.
- This capability enhances its ability to thrive in nitrogen-limited wine environments.
- Findings have significant implications for wine nitrogen management and O. oeni's ecological role.
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