title: Heating and reduction affect the reaction with tannins of wine protein fractions differing in hydrophobicity.
abstract: During the storage, bottled white wines can manifest haziness due to the insolubilisation of the grape proteins that may 'survive' in the fermentation process. Although the exact mechanism of this occurrence is not fully understood, proteins and tannins are considered two of the key factors involved in wine hazing, since their aggregation leads to the formation of insoluble particles. To better understand this complex interaction, proteins and tannins from the same unfined Pinot grigio wine were separated. Wine proteins were then fractionated by hydrophobic interaction chromatography (HIC). A significant correlation between hydrophobicity of the wine protein fractions and the haze formed after reacting with wine tannins was found, with the most reactive fractions revealing (by SDS-PAGE and RP-HPLC analyses) the predominant presence of thaumatin-like proteins. Moreover, the effects of both protein heating and disulfide bonds reduction (with dithiotreithol) on haze formation in the presence of tannins were assessed. These treatments generally resulted in an improved reactivity with tannins, and this phenomenon was related to both the surface hydrophobicity and composition of the protein fractions. Therefore, haze formation in wines seems to be related to hydrophobic interactions occurring among proteins and tannins. These interactions should occur on hydrophobic tannin-binding sites, whose exposition on the proteins can depend on both protein heating and reduction.
authors.affiliation: Dipartimento di Biotecnologie agrarie and Centro Interdipartimentale per la Ricerca in Viticoltura ed Enologia (C.I.R.V.E.) Università di Padova, via dell'Università 16, 35020 Legnaro (PD), Italy.
authors.forename: Matteo
authors.initials: M
authors.lastname: Marangon
authors.forename: Simone
authors.initials: S
authors.lastname: Vincenzi
authors.forename: Marco
authors.initials: M
authors.lastname: Lucchetta
authors.forename: Andrea
authors.initials: A
authors.lastname: Curioni
mesh_terms: D002853:Chromatography, Liquid; D057927:Hydrophobic and Hydrophilic Interactions; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011485:Protein Binding; D013438:Sulfhydryl Compounds / Q000737:chemistry; D013634:Tannins / Q000737:chemistry*; D013696:Temperature; D014920:Wine / Q000032:analysis*
chemical_list: D010940:Plant Proteins; D013438:Sulfhydryl Compounds; D013634:Tannins