Understanding the molecular interactions between a yeast protein extract and phenolic compounds. (May 2021)

• Record Type: Journal Article
• Authors: Francisco, Telmo; Pérez-Gregorio, Rosa; Soares, Susana; Mateus, Nuno; Centeno, Filipe; de Fátima Teixeira, Maria; de Freitas, Victor
• Is Part Of: Food research international. Volume 143(2021)
• Publication Date: 2021-05
• Subjects: Polyphenol-protein interactions -- Plant-based beverages -- Astringency -- Bitterness -- Fining -- Fluorescence quenching; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2021.110261
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphical abstract: Highlights: The interaction between polyphenols & a new yeast protein extract (YPE) was studied. Pentagalloylglucose had the highest binding affinity followed by malvidin 3-glucoside. Interaction affinities and size of aggregates were affected by temperature and solvent. Binding selectivity of proteins from YPE was not found. Abstract: Phenolic compounds are partially removed during fining, which may influence the organoleptic properties of beverages. Among phenolic compounds, tannins have been widely associated to the taste of beverages (namely astringency and bitterness). Furthermore, phenolic acids and anthocyanins may also influence bitterness and the latter are also responsible for beverages' color. Thus, it is necessary to perform molecular studies to better understand the effect of fining agents in the overall phenolic composition of beverages and the resulting organoleptic changes. The molecular interactions between these three classes of phenolic compounds and a yeast protein extract (YPE), designed as a new fining agent, was studied. The binding affinities were assessed by fluorescence quenching at two temperatures (21 °C and 37 °C) and in two reaction media (water and wine model solution). The size of aggregates formed was characterized by Dynamic Light Scattering and the selectivity of protein interaction was analyzed by electrophoresis. Overall, pentagalloylglucoside (tannin) showed the highest binding affinity for YPE, followed by malvidin 3-glucoside (anthocyanin), p -coumaric acid (phenolic acid) and gallic acid (phenolic acid). The studied temperatures and solvents affected the interaction affinities as well as the aggregates' size. Binding selectivity of proteins from YPE was not found. These results open new perspectives to control the fining process by using the YPE as a fining agent taking into account the further effect in the organoleptic properties of beverages.