Capture depletion of grapevine DNA: an approach to advance the study of microbial community in wine

During red wine ageing or conservation, color and taste change and astringency tends to reduce. These changes result from reactions of flavan-3-ols and/or anthocyanins among which condensation reactions with acetaldehyde are particularly important. The full characterization of these reactions has not been fully achieved because of difficulties in extracting and separating the newly formed compounds directly from wine. Model solutions mimicking food products constitute a simplified medium for their exploration, allowing the detection of the newly formed compounds, their isolation, and their structure elucidation.

Proteins constitute one of the three main components of grape juice and white wine, phenolic compounds and polysaccharides being the others. A specific group of the total grape-derived proteins resists degradation or adsorption during the winemaking process and remains in finished wine if not removed by the commonplace commercial practice of bentonite fining. While bentonite is effective in removing the problematic proteins, it is claimed to adversely affect the quality of the treated wine under certain conditions, through the removal of colour, flavor and texture compounds. A number of studies have indicated that different protein fractions require distinct bentonite concentrations for protein removal and consequent heat stabilization.

Despite the extensive research performed during the last decades, the multifactorial mechanism responsible for the white wine protein haze formation is not fully characterized. Herein, a new model is proposed, which is based on the experimental identification of sulfur dioxide as a major modulating factor inducing wine protein haze upon heating. As opposed to other reducing agents, such as 2-mercaptoethanol, dithiothreitol and tris(2-carboxyethyl)phosphine hydrochloride (TCEP), the addition of SO2 to must/wine upon heating cleaves intraprotein disulfide bonds, hinders thiol-disulfide exchange during protein interactions and can lead to the formation of novel inter/intraprotein disulfide bonds. Those are eventually responsible for wine protein aggregation which follows a nucleation-growth kinetic model as shown by dynamic light scattering [1].

Yeast cells possess a cell wall comprising primarily glycoproteins, mannans, and glucan polymers. Several yeast phenotypes relevant for fermentation, wine processing, and wine quality are correlated with cell wall properties. To investigate the effect of wine fermentation on cell wall composition, a study was performed using mid-infrared (MIR) spectroscopy coupled with multivariate methods (i.e., PCA and OPLS-DA). A total of 40 yeast strains were evaluated, including Saccharomyces strains (laboratory and industrial) and non-Saccharomyces species. Cells were fermented in both synthetic MS300 and Chardonnay grape must to stationery phase, processed, and scanned in the MIR spectrum.

Volatile thiols contribute largely to the organoleptic characteristics and typicity of Sauvignon blanc wines. Among this family of odorous compounds, 3-sulfanylhexan-1-ol (3SH) and 4-methyl-4-sulfanylpentan-2-one (4MSP) have a major impact on wine flavor. These thiols are formed during alcoholic fermentation by the yeast from odorless and non-volatile precursors found in the berry and the must. The effect of vine nitrogen status on 3SH and 4MSP in Sauvignon blanc wine and on the glutathionylated and cysteinylated precursors of 3SH (Glut-3SH and Cys-3SH) was investigated in this study.