Plant proteins have been proposed as an alternative to animal-origin proteins in the wine industry because they are allergen-free and vegan-friendly. The aim of this study was to evaluate the effectiveness of plant proteins as fining agents on red wines with different phenolic composition. Two formulations for commercially available vegetal proteins (potato and pea origin) were assessed at two doses to modulate the fining treatment to the wine phenolic profile. The results evidenced that fining agents derived from plants have different levels of effectiveness on the removal of phenolic compounds depending on the origin, the formulation used, dose applied, and also wine characteristics. On Nebbiolo wine, the study was particularly significant due to its phenolic composition. One pea-based fining agent had an effect comparable to gelatin (animal origin) on the removal of polymeric flavanols with a minor loss of anthocyanins and therefore better preserving the wine color in terms of intensity and hue. For Primitivo, Montepulciano, and Syrah wines, even though there was a formulation-dependent effect, vegetal proteins gave more balanced reductions in terms of target phenolic compounds contributing to astringency and color perception.Molecules 2020, 25, 120 2 of 20 isolated from cereals, legumes, potatoes [6,7], seaweeds, grape seed extracts [8,9], and yeasts [10,11]. Other vegetal non-proteinaceous products, such as polysaccharide-based agents isolated from cell wall material of fresh apples and grapes or their respective pomaces, have shown great potential for wine fining purposes [12][13][14][15].Focusing on protein-based fining agents, they can have a different affinity to different types of phenolic compounds. Proteins interact with wine phenolic compounds initially through hydrogen bonding and hydrophobic interactions, forming soluble complexes. In fact, gelatin is a highly efficient fining agent because of its potential hydrogen binding sites [3]. Subsequently, phenolic compounds are removed by precipitation through self-association of the complexes formed [16] or formation of insoluble protein aggregates (cross-linkages between proteins) incorporating the target species [17]. This precipitation induces reduced astringency and depends on the protein to tannin ratio as well as on the amino acid composition, tertiary structure, hydrophobicity, and molecular mass of proteins [2,18]. It is well-known that proline-rich proteins have a strong affinity to phenolic compounds and therefore they are of great interest for wine fining [19]. Concretely, aromatic ring structures of phenolic compounds have hydrophobic properties and the presence of galloylated units enhances the hydrophobic interactions with proline-rich proteins [20].Among allergen-free vegetal proteins isolated from cereals, corn zeins are a heterogeneous protein mixture made of polypeptides differing in molecular mass, aggregation state, and isoelectric point. The effectiveness of zein as a fining agent could be due to their relative hydrophobicity, which ...