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Mass spectrometry-based proteomic approach in Oenococcus oeni enological starter
Anna Napoli1, Donatella Aiello, Gilda Aiello
1Department of Chemistry and Chemical Technologies, University of Calabria , Via P. Bucci, Cubo 12/D, 87036 Arcavacata di Rende (CS), Italy.
Journal of Proteome Research
|April 29, 2014
Summary
This study introduces a streamlined method for analyzing Oenococcus oeni (O. oeni) proteins using LC-MALDI MS. The analysis identified key proteins, mutations, and phosphorylation sites, offering insights into bacterial cell functions.
Area of Science:
- Microbiology
- Proteomics
- Biochemistry
Background:
- Oenococcus oeni (O. oeni) is a key bacterium in winemaking, but its proteome is not fully characterized.
- Understanding O. oeni's cytoplasmic and membrane-related proteins (MRP) is crucial for optimizing fermentation processes.
Purpose of the Study:
- To develop a simple and effective procedure for selective protein solubilization and digestion of O. oeni.
- To identify and characterize O. oeni proteins, including post-translational modifications and mutations, using LC-MALDI MS.
- To investigate protein microheterogeneity in O. oeni.
Main Methods:
- Selective protein solubilization and trypsin digestion.
- Off-line liquid chromatography-matrix assisted laser desorption ionization mass spectrometry (LC-MALDI MS).
- Peptide identification via tandem mass spectrometry (MS/MS) and database searching.
Main Results:
- Identification of cytoplasmic and membrane-related proteins (MRP) in O. oeni.
- Discovery of 13 peptides with single-point mutations across 9 proteins.
- Detailed characterization of microheterogeneity in Zn-dependent alcohol dehydrogenase (Zn-ADH) and 60 kDa chaperonin (GroEL).
- Identification of 34 unique phosphorylation sites on 19 phosphoproteins.
Conclusions:
- The proposed LC-MALDI MS method is effective for comprehensive O. oeni proteome analysis.
- The study reveals significant protein microheterogeneity and post-translational modifications in O. oeni.
- Findings provide valuable insights into O. oeni's cellular functions and adaptability.
