Work

Screening of wine industry by-products as a source of bioactive peptides: Fractionation, in vitro antihypertensive activity and peptidomics analysis

Year: 2025

Type: article

Abstract: The suitability of grape pomace and wine lees protein isolates as a source of bioactive peptides with antihypertensive activity was evaluated through hydrolysis with different proteolytic enzymes. Peptides were initially fractionated by ultrafiltration. The determination of the angiotensin-converting enzyme inhibitory activity evidenced that hydrolysates of Flavourzyme from grape pomace and of Alcalase from wine lees showed higher bioactivities. The fractions <3 kDa of these hydrolysates were further purified by semipreparative reversed-phase liquid chromatography. The peptidome of the fractions showing the highest angiotensin-converting enzyme inhibitory activities was characterised by nano-liquid chromatography-Orbitrap tandem mass spectrometry. The analysis of the chemical features of identified peptides like hydrophobicity and the frequency of angiotensin-converting enzyme inhibitory-active di-, tri- and tetrapeptide motives was associated with the antihypertensive activity. The peptides GPCKFYYGK, FSSFYYGK and YYGKF, among others, appear to contribute significantly to the antihypertensive activity of the hydrolysates. • Grape pomace and wine lees protein hydrolysates showed different ACEi activities • Peptides in the most active ACEi fractions were identified by nano-LC-Orbitrap MS/MS • Hydrophobicity and ACEi-active motives were linked with the antihypertensive activity • Amino acid composition of identified peptides predicted the bioactivity of fractions • High frequency tetrapeptides were found in most active fractions

Source: Food Chemistry

DOI: 10.1016/j.foodchem.2025.143478

Authors: Ariel Fontana, Franziska Knuf, Romina Monasterio, Andreas Schieber