期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 60, 期 42, 页码 10666-10673出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf302916n
关键词
aggregation; chitinase; haze; phenolics; polysaccharides; protein stability; thaumatin-like protein; white wine
资金
- Grape and Wine Research and Development Corporation
- Australian government
- Provincia di Treviso (Italy)
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.
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