Effect of different yeast mannoproteins on the interaction between wine flavanols and salivary proteins
Autor: | Alba M. Ramos-Pineda, Ignacio García-Estévez, Elvira Manjón, M. Teresa Escribano-Bailón, Alberto Recio-Torrado |
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Rok vydání: | 2021 |
Předmět: |
Wine
0303 health sciences Membrane Glycoproteins 030309 nutrition & dietetics Chemistry Polyphenols Saccharomyces cerevisiae 04 agricultural and veterinary sciences Protein aggregation Degree of polymerization 040401 food science High-performance liquid chromatography Yeast 03 medical and health sciences 0404 agricultural biotechnology Dynamic light scattering Salivary Proteins Humans Composition (visual arts) Food science Salivary Proteins and Peptides Food Science |
Zdroj: | Food Research International. 143:110279 |
ISSN: | 0963-9969 |
Popis: | Unbalanced wine astringency, caused by a gap between phenolic and technological grape maturities, is one of the consequences of the global climate change in the vitiviniculture. To resolve it, potential strategies are being currently used, like the addition of commercial yeast mannoproteins (MPs) to wines. In this work, the main interactions responsible for the wine astringent sensation, namely, interactions between human salivary proteins and wine flavanols have been studied by Dynamic Light Scattering (DLS) and liquid chromatography coupled to DAD and MS detectors (HPLC-DAD-MS), in presence or absence of two MPs with different saccharide/protein ratio. The results indicate that there are differences on the substrate specificity for each mannoprotein and that its action mechanism could change not only depending on the mannoprotein composition but also on the flavanol structure. MPs with elevated carbohydrate content could act thought the stabilization of soluble aggregates with human salivary proteins and flavanols, mainly non-galloylated flavanol oligomers, whereas MPs with higher protein percentage mostly could precipitate flavanols (mainly non-galloylated ones with low degree of polymerization) which partially prevents the formation of insoluble flavanol-salivary protein aggregates. |
Databáze: | OpenAIRE |
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