Roles of Proteins, Polysaccharides, and Phenolics in Haze Formation in White Wine via Reconstitution Experiments

被引:57
作者
Gazzola, Diana [2 ]
Van Sluyter, Steven C. [3 ]
Curioni, Andrea [2 ]
Waters, Elizabeth J. [1 ]
Marangon, Matteo [1 ]
机构
[1] Australian Wine Res Inst, Adelaide, SA 5064, Australia
[2] Univ Padua, Dept Agron Food Nat Resources Anim & Environm, Ctr Interdipartimentale Ric Viticoltura Enol CIRV, I-35020 Legnaro, PD, Italy
[3] Macquarie Univ, Dept Chem & Biomol Sci, Sydney, NSW 2109, Australia
关键词
aggregation; chitinase; haze; phenolics; polysaccharides; protein stability; thaumatin-like protein; white wine; STABILITY; AGGREGATION; TEMPERATURE; TANNINS; SIZE;
D O I
10.1021/jf302916n
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
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 degrees C for 1 h and 25 degrees 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.
引用
收藏
页码:10666 / 10673
页数:8
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