Influence of the reducing environment in the misfolding of wine proteins.
Identifieur interne : 000037 ( Main/Exploration ); précédent : 000036; suivant : 000038Influence of the reducing environment in the misfolding of wine proteins.
Auteurs : Paolo Ruzza [Italie] ; Claudia Honisch [Italie] ; Matteo Marangon [Italie] ; Andrea Curioni [Italie] ; Alan Bakalinsky [États-Unis] ; Simone Vincenzi [Italie]Source :
- Advances in protein chemistry and structural biology [ 1876-1631 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- analyse : Vin.
- composition chimique : Protéines végétales.
- métabolisme : Protéines végétales.
- Pliage des protéines, Similitude de séquences d'acides aminés, Stabilité protéique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plant Proteins.
- chemical , metabolism : Plant Proteins.
- analysis : Wine.
- Amino Acid Sequence, Protein Folding, Protein Stability, Sequence Homology, Amino Acid.
Abstract
While proteins are present in wine at low concentration, and are largely associated with undesirable haze formation in white wines, certain types or fractions make direct and indirect contributions to sensory quality and physical stability. The proteins found in wine represent a small subclass of the total pool of grape proteins that remain soluble in the non-physiological conditions of the wine matrix which is characterised by the presence of alcohol, high acidity, and relatively high levels of phenolic compounds. Although initially stable in these conditions, during storage of white and rosé wines proteins undergo changes leading to haze formation which is considered one of the most relevant non-microbiological defects, and which makes the wine commercially unacceptable. This phenomenon involves the two most abundant proteins present in wines: thaumatin-like proteins and chitinases, both belonging to pathogenesis-related proteins of the grape berry. Haze formation is often triggered by thermal fluctuations occurring during storage of white wines, although the presence of other non-protein-related factors seems to be necessary. Here, we review the characteristics of these two protein families and the factors that influence their solubility with a focus on the disulfide bonds reduction as a possible trigger for the onset of their aggregation.
DOI: 10.1016/bs.apcsb.2019.08.004
PubMed: 31928733
Affiliations:
Links toward previous steps (curation, corpus...)
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Department of Chemical Sciences, University of Padua, Padova, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Biomolecular Chemistry of CNR, Padua Unit, Padova, Italy; Department of Chemical Sciences, University of Padua, Padova</wicri:regionArea><wicri:noRegion>Padova</wicri:noRegion></affiliation></author><author><name sortKey="Marangon, Matteo" sort="Marangon, Matteo" uniqKey="Marangon M" first="Matteo" last="Marangon">Matteo Marangon</name><affiliation wicri:level="1"><nlm:affiliation>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV), Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV)</wicri:regionArea><wicri:noRegion>Conegliano (TV)</wicri:noRegion></affiliation></author><author><name sortKey="Curioni, Andrea" sort="Curioni, Andrea" uniqKey="Curioni A" first="Andrea" last="Curioni">Andrea Curioni</name><affiliation wicri:level="1"><nlm:affiliation>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV), Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV)</wicri:regionArea><wicri:noRegion>Conegliano (TV)</wicri:noRegion></affiliation></author><author><name sortKey="Bakalinsky, Alan" sort="Bakalinsky, Alan" uniqKey="Bakalinsky A" first="Alan" last="Bakalinsky">Alan Bakalinsky</name><affiliation wicri:level="2"><nlm:affiliation>Department of Food Science and Technology, Oregon State University, Corvallis, Oregon, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Food Science and Technology, Oregon State University, Corvallis, Oregon</wicri:regionArea><placeName><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Vincenzi, Simone" sort="Vincenzi, Simone" uniqKey="Vincenzi S" first="Simone" last="Vincenzi">Simone Vincenzi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV), Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV)</wicri:regionArea><wicri:noRegion>Conegliano (TV)</wicri:noRegion></affiliation></author></analytic><series><title level="j">Advances in protein chemistry and structural biology</title><idno type="eISSN">1876-1631</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Protein Folding (MeSH)</term><term>Protein Stability (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Wine (analysis)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Pliage des protéines (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Stabilité protéique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Vin (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Vin</term></keywords><keywords scheme="MESH" qualifier="analysis" xml:lang="en"><term>Wine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Protein Folding</term><term>Protein Stability</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Pliage des protéines</term><term>Similitude de séquences d'acides aminés</term><term>Stabilité protéique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">While proteins are present in wine at low concentration, and are largely associated with undesirable haze formation in white wines, certain types or fractions make direct and indirect contributions to sensory quality and physical stability. The proteins found in wine represent a small subclass of the total pool of grape proteins that remain soluble in the non-physiological conditions of the wine matrix which is characterised by the presence of alcohol, high acidity, and relatively high levels of phenolic compounds. Although initially stable in these conditions, during storage of white and rosé wines proteins undergo changes leading to haze formation which is considered one of the most relevant non-microbiological defects, and which makes the wine commercially unacceptable. This phenomenon involves the two most abundant proteins present in wines: thaumatin-like proteins and chitinases, both belonging to pathogenesis-related proteins of the grape berry. Haze formation is often triggered by thermal fluctuations occurring during storage of white wines, although the presence of other non-protein-related factors seems to be necessary. Here, we review the characteristics of these two protein families and the factors that influence their solubility with a focus on the disulfide bonds reduction as a possible trigger for the onset of their aggregation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31928733</PMID><DateCompleted><Year>2020</Year><Month>04</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1876-1631</ISSN><JournalIssue CitedMedium="Internet"><Volume>118</Volume><PubDate><Year>2019</Year></PubDate></JournalIssue><Title>Advances in protein chemistry and structural biology</Title><ISOAbbreviation>Adv Protein Chem Struct Biol</ISOAbbreviation></Journal><ArticleTitle>Influence of the reducing environment in the misfolding of wine proteins.</ArticleTitle><Pagination><MedlinePgn>413-436</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1876-1623(19)30058-6</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/bs.apcsb.2019.08.004</ELocationID><Abstract><AbstractText>While proteins are present in wine at low concentration, and are largely associated with undesirable haze formation in white wines, certain types or fractions make direct and indirect contributions to sensory quality and physical stability. The proteins found in wine represent a small subclass of the total pool of grape proteins that remain soluble in the non-physiological conditions of the wine matrix which is characterised by the presence of alcohol, high acidity, and relatively high levels of phenolic compounds. Although initially stable in these conditions, during storage of white and rosé wines proteins undergo changes leading to haze formation which is considered one of the most relevant non-microbiological defects, and which makes the wine commercially unacceptable. This phenomenon involves the two most abundant proteins present in wines: thaumatin-like proteins and chitinases, both belonging to pathogenesis-related proteins of the grape berry. Haze formation is often triggered by thermal fluctuations occurring during storage of white wines, although the presence of other non-protein-related factors seems to be necessary. Here, we review the characteristics of these two protein families and the factors that influence their solubility with a focus on the disulfide bonds reduction as a possible trigger for the onset of their aggregation.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ruzza</LastName><ForeName>Paolo</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institute of Biomolecular Chemistry of CNR, Padua Unit, Padova, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Honisch</LastName><ForeName>Claudia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institute of Biomolecular Chemistry of CNR, Padua Unit, Padova, Italy; Department of Chemical Sciences, University of Padua, Padova, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Marangon</LastName><ForeName>Matteo</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV), Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Curioni</LastName><ForeName>Andrea</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV), Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bakalinsky</LastName><ForeName>Alan</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Food Science and Technology, Oregon State University, Corvallis, Oregon, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vincenzi</LastName><ForeName>Simone</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Agronomy, Food, Natural Resources, Animals and Environment (DAFNAE), University of Padua, Legnaro (PD), Italy; Centre for Research in Viticulture and Enology (CIRVE), Conegliano (TV), Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>10</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Adv Protein Chem Struct Biol</MedlineTA><NlmUniqueID>101497281</NlmUniqueID><ISSNLinking>1876-1623</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014920" MajorTopicYN="N">Wine</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Chitinases</Keyword><Keyword MajorTopicYN="Y">Circular dichroism</Keyword><Keyword MajorTopicYN="Y">Fluorescence</Keyword><Keyword MajorTopicYN="Y">NMR</Keyword><Keyword MajorTopicYN="Y">Protein misfolding</Keyword><Keyword MajorTopicYN="Y">Reducing agents</Keyword><Keyword MajorTopicYN="Y">Thaumatin-like proteins</Keyword><Keyword MajorTopicYN="Y">Wine haze</Keyword><Keyword MajorTopicYN="Y">Wine instability factors</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>1</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>1</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31928733</ArticleId><ArticleId IdType="pii">S1876-1623(19)30058-6</ArticleId><ArticleId IdType="doi">10.1016/bs.apcsb.2019.08.004</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li><li>États-Unis</li></country><region><li>Oregon</li></region></list><tree><country name="Italie"><noRegion><name sortKey="Ruzza, Paolo" sort="Ruzza, Paolo" uniqKey="Ruzza P" first="Paolo" last="Ruzza">Paolo Ruzza</name></noRegion><name sortKey="Curioni, Andrea" sort="Curioni, Andrea" uniqKey="Curioni A" first="Andrea" last="Curioni">Andrea Curioni</name><name sortKey="Honisch, Claudia" sort="Honisch, Claudia" uniqKey="Honisch C" first="Claudia" last="Honisch">Claudia Honisch</name><name sortKey="Marangon, Matteo" sort="Marangon, Matteo" uniqKey="Marangon M" first="Matteo" last="Marangon">Matteo Marangon</name><name sortKey="Vincenzi, Simone" sort="Vincenzi, Simone" uniqKey="Vincenzi S" first="Simone" last="Vincenzi">Simone Vincenzi</name></country><country name="États-Unis"><region name="Oregon"><name sortKey="Bakalinsky, Alan" sort="Bakalinsky, Alan" uniqKey="Bakalinsky A" first="Alan" last="Bakalinsky">Alan Bakalinsky</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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