Mass spectrometry in the analysis of grape and wine proteins.
Expert Rev Proteomics. 2006 Jun; 3(3):321-31.ER

Abstract

Wine proteins play an important role in the quality of wine, because they affect taste, clarity and stability of product. The majority of wine proteins are in the range of 20-30 kDa. Different mass spectrometry (MS) techniques have been successfully applied to study the grape and wine proteins. By liquid chromatography (LC) electrospray ionization (ESI) MS and nano-LC/MS, nine dipeptides and 80 peptides were unambiguously identified in Champagne and Sauvignon Blanc wines, respectively. Using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) and surface-enhanced laser desorption/ionization TOF, the protein and peptide fingerprints in Chardonnay, Sauvignon Blanc and Muscat of Alexandria wines were determined. MALDI-TOF identified the mesocarp proteome of six Vitis grape varieties. Proteins in different grape tissue extracts were also studied. The major grape pathogenic-related proteins are chitinases and thaumatin-like proteins, which both persist through the vinification process and cause hazes and sediments in bottled wines. ESI-MS, LC/ESI-MS and MALDI-TOF analysis of these proteins in grape and wine were also used to characterize different grape varieties.

Authors+Show Affiliations

Flamini R

Quality Control of Wine at the Agricultural Faculty of Padua University, Italy. riccardo.flamini@ispervit.it

De Rosso M

No affiliation info available

MeSH

Food IndustryMass SpectrometryProteinsVitisWine

Pub Type(s)

Journal Article

Review

Language

eng

PubMed ID

16771704

Citation

Flamini, Riccardo, and Mirko De Rosso. "Mass Spectrometry in the Analysis of Grape and Wine Proteins." Expert Review of Proteomics, vol. 3, no. 3, 2006, pp. 321-31.

Flamini R, De Rosso M. Mass spectrometry in the analysis of grape and wine proteins. Expert Rev Proteomics. 2006;3(3):321-31.

Flamini, R., & De Rosso, M. (2006). Mass spectrometry in the analysis of grape and wine proteins. Expert Review of Proteomics, 3(3), 321-31.

Flamini R, De Rosso M. Mass Spectrometry in the Analysis of Grape and Wine Proteins. Expert Rev Proteomics. 2006;3(3):321-31. PubMed PMID: 16771704.

* Article titles in AMA citation format should be in sentence-case

TY - JOUR T1 - Mass spectrometry in the analysis of grape and wine proteins. AU - Flamini,Riccardo, AU - De Rosso,Mirko, PY - 2006/6/15/pubmed PY - 2006/8/5/medline PY - 2006/6/15/entrez SP - 321 EP - 31 JF - Expert review of proteomics JO - Expert Rev Proteomics VL - 3 IS - 3 N2 - Wine proteins play an important role in the quality of wine, because they affect taste, clarity and stability of product. The majority of wine proteins are in the range of 20-30 kDa. Different mass spectrometry (MS) techniques have been successfully applied to study the grape and wine proteins. By liquid chromatography (LC) electrospray ionization (ESI) MS and nano-LC/MS, nine dipeptides and 80 peptides were unambiguously identified in Champagne and Sauvignon Blanc wines, respectively. Using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) and surface-enhanced laser desorption/ionization TOF, the protein and peptide fingerprints in Chardonnay, Sauvignon Blanc and Muscat of Alexandria wines were determined. MALDI-TOF identified the mesocarp proteome of six Vitis grape varieties. Proteins in different grape tissue extracts were also studied. The major grape pathogenic-related proteins are chitinases and thaumatin-like proteins, which both persist through the vinification process and cause hazes and sediments in bottled wines. ESI-MS, LC/ESI-MS and MALDI-TOF analysis of these proteins in grape and wine were also used to characterize different grape varieties. SN - 1744-8387 UR - https://www.unboundmedicine.com/medline/citation/16771704/Mass_spectrometry_in_the_analysis_of_grape_and_wine_proteins_ DB - PRIME DP - Unbound Medicine ER -

Tags

Mass spectrometry in the analysis of grape and wine proteins.Expert Rev Proteomics. 2006 Jun; 3(3):321-31.ER