Abstract
AbstractSparkling wine is an alcoholic beverage enjoyed around the world. The sensory properties of sparkling wine depend on a complex interplay between the chemical and biochemical components in the final product. Glycoproteins have been linked to positive and negative qualities in sparkling wine, but the glycosylation profiles of sparkling wine have not been previously investigated in detail. We analyzed the glycoproteome of sparkling wines using protein- and glycopeptide-centric approaches. We developed an automated workflow that created ion libraries to analyze sequential window acquisition of all theoretical mass spectra data-independent acquisition mass spectrometry data based on glycopeptides identified by Byonic (Protein Metrics; version 2.13.17). We applied our workflow to three pairs of experimental sparkling wines to assess the effects of aging on lees and of different yeast strains used in the liqueur de tirage for secondary fermentation. We found that aging a cuvée on lees for 24 months compared with 8 months led to a dramatic decrease in overall protein abundance and an enrichment in large glycans at specific sites in some proteins. Secondary fermentation of a Riesling wine with Saccharomyces cerevisiae yeast strain Siha4 produced more yeast proteins and glycoproteins than with S. cerevisiae yeast strain DV10. The abundance and glycosylation profiles of grape glycoproteins were also different between grape varieties. To our knowledge, this work represents the first in-depth study into protein- and peptide-specific glycosylation in sparkling wines and describes a quantitative glycoproteomic sequential window acquisition of all theoretical mass spectra/data-independent acquisition workflow that is broadly applicable to other sample types.
Highlights
Application to three pairs of commercial-scale experimental sparkling wines. Decreased protein abundance in cuvee during the aging process. Different yeast strains produce varying levels of yeast proteins
Preliminary LC–mass spectrometry (MS)/MS proteomic investigations of tryptic digests of sparkling wines revealed that the dominant components in these samples were glycopeptides (Fig. 2), with precursor masses separated by 162 Da (Hex) and 132 Da (Pent) and MS/MS spectra containing ions corresponding to oxonium ions for hexose and pentose
Little difference was observed in the abundance of glycoforms from the glycopeptides ER/VN/LVELGVYVSDIR shared in all 24 seripauperins (Fig. 6D)
Summary
Application to three pairs of commercial-scale experimental sparkling wines. Decreased protein abundance in cuvee during the aging process. Different yeast strains produce varying levels of yeast proteins. Despite the low concentration (4–20 mg/l) (6) of proteins and glycoproteins in wine and sparkling wine, they are especially important for determining its sensory properties. They can alter the clarity and stability (7–9) and positively influence foaming (10). Saccharomyces cerevisiae yeast produces high mannose N-linked and oligomannose O-linked glycans attached to the side-chain amide of Asn and the hydroxyl groups of Ser or Thr, respectively (19). This oligomannose O-glycosylation has been observed on proteins in sparkling. O-linked glycans on grape glycoproteins are commonly attached through the hydroxyl group of hydroxyproline and contain predominately arabinose and/or galactose (21, 22)
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