Roles of proteins, polysaccharides, and phenolics in haze formation in white wine via reconstitution experiments

Residual proteins in finished wines can aggregate to form haze. To obtain insights into the mechanism of protein haze formation, a reconstitution approach was used to study the heat-induced aggregation behavior of purified wine proteins. A chitinase, four thaumatin-like protein (TLP) isoforms, phenolics, and polysaccharides were isolated from a Chardonnay wine. The same wine was stripped of these compounds and used as a base to reconstitute each of the proteins alone or in combination with the isolated phenolics and/or polysaccharides. After a heating and cooling cycle (70 °C for 1 h and 25 °C for 15 h), the size and concentration of the aggregates formed were measured by scanning ion occlusion sensing (SIOS), a technique to detect and quantify nanoparticles. The chitinase was the protein most prone to aggregate and the one that formed the largest particles; phenolics and polysaccharides did not have a significant impact on its aggregation behavior. TLP isoforms varied in susceptibility to haze formation and in interactions with polysaccharides and phenolics. The work establishes SIOS as a useful method for studying wine haze.