Effect of plant fining agents in the must flotation process. Functional characterization

Abstract

Flotation is one of the most used processes for clarifying white grape must after the pressing process. To date, gelatine is the more used fining agent, its action being improved when combined with bentonite and silica sol. However, in recent years, there is a growing commercial interest in replacing this animal origin protein with plant proteins, due, on the one hand, to the problems associated with allergies and, on the other hand, also thinking in the vegan wine consumers. However the efficiency of plant proteins as floculating agents are lower than gelatine and varies among them, the reason behind the different behaviour being unknown (Marchal et al., 2003; Gambuti et al., 2016; Petinelli et al., 2020). The objective of this work was to compare the flocculating efficiency of a commercial gelatine, a pure pea protein and the same pea protein chemically modified and to relate this efficiency to their amino acid composition and protein functions.The determination of the efficiency was carried out by measuring the percentage of clean must after 1 h from flotation beginning and the measuring of the absorbance at 440 nm to control the browning, while the content of amino acids and peptides was carried out by HPLC-MS. The UNIPROT database was used to obtain the protein functions associated with the peptidesThe results showed that the modified pea protein showed very similar effciency as flotation agent to that of the commercial gelatine and higher than the pure pea protein. The important structural modification made to the pea protein made it more reactive, probably due to a higher exposure of its structure and the apolar and positively charged amino acids, and to the appearance of peptides with protein functions of binding to carbohydrates and proteins, which are also present in animal protein. With these results it can be concluded that pure vegetal proteins may not have sufficientt functional properties to behave as good flocculating agents, although certain chemical modification in their structure may further simulate the behaviour shown by animal protein.