Roles of proteins, polysaccharides, and phenolics in haze formation in white wine via reconstitution experiments.
Identifieur interne : 000214 ( Main/Curation ); précédent : 000213; suivant : 000215Roles of proteins, polysaccharides, and phenolics in haze formation in white wine via reconstitution experiments.
Auteurs : Diana Gazzola [Italie] ; Steven C. Van Sluyter ; Andrea Curioni ; Elizabeth J. Waters ; Matteo MarangonSource :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2012.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Phenols, Polysaccharides, Proteins.
- analysis : Wine.
- Chromatography, High Pressure Liquid, Temperature.
Abstract
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.
DOI: 10.1021/jf302916n
PubMed: 22998638
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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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22998638</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>16</Day></DateCompleted><DateRevised><Year>2012</Year><Month>10</Month><Day>29</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5118</ISSN><JournalIssue CitedMedium="Internet"><Volume>60</Volume><Issue>42</Issue><PubDate><Year>2012</Year><Month>Oct</Month><Day>24</Day></PubDate></JournalIssue><Title>Journal of agricultural and food chemistry</Title><ISOAbbreviation>J Agric Food Chem</ISOAbbreviation></Journal><ArticleTitle>Roles of proteins, polysaccharides, and phenolics in haze formation in white wine via reconstitution experiments.</ArticleTitle><Pagination><MedlinePgn>10666-73</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jf302916n</ELocationID><Abstract><AbstractText>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. 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