Sulfur dioxide induced aggregation of wine thaumatin-like proteins: Role of disulfide bonds.
Identifieur interne : 000059 ( Main/Exploration ); précédent : 000058; suivant : 000060Sulfur dioxide induced aggregation of wine thaumatin-like proteins: Role of disulfide bonds.
Auteurs : Ricardo Chagas [Portugal] ; César A T. Laia [Portugal] ; Ricardo B. Ferreira [Portugal] ; Luísa M. Ferreira [Portugal]Source :
- Food chemistry [ 1873-7072 ] ; 2018.
Descripteurs français
- KwdFr :
- Agrégats de protéines (effets des médicaments et des substances chimiques), Chromatographie sur gel (MeSH), Dichroïsme circulaire (MeSH), Diffusion dynamique de la lumière (MeSH), Dioxyde de soufre (composition chimique), Dioxyde de soufre (pharmacologie), Disulfures (composition chimique), Interactions hydrophobes et hydrophiles (MeSH), Protéines végétales (composition chimique), Protéines végétales (isolement et purification), Protéines végétales (métabolisme), Spectrométrie de fluorescence (MeSH), Température (MeSH), Vin (analyse).
- MESH :
- analyse : Vin.
- composition chimique : Dioxyde de soufre, Disulfures, Protéines végétales.
- effets des médicaments et des substances chimiques : Agrégats de protéines.
- isolement et purification : Protéines végétales.
- métabolisme : Protéines végétales.
- pharmacologie : Dioxyde de soufre.
- Chromatographie sur gel, Dichroïsme circulaire, Diffusion dynamique de la lumière, Interactions hydrophobes et hydrophiles, Spectrométrie de fluorescence, Température.
English descriptors
- KwdEn :
- Chromatography, Gel (MeSH), Circular Dichroism (MeSH), Disulfides (chemistry), Dynamic Light Scattering (MeSH), Hydrophobic and Hydrophilic Interactions (MeSH), Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (metabolism), Protein Aggregates (drug effects), Spectrometry, Fluorescence (MeSH), Sulfur Dioxide (chemistry), Sulfur Dioxide (pharmacology), Temperature (MeSH), Wine (analysis).
- MESH :
- chemical , chemistry : Disulfides, Plant Proteins, Sulfur Dioxide.
- chemical , drug effects : Protein Aggregates.
- chemical , isolation & purification : Plant Proteins.
- chemical , metabolism : Plant Proteins.
- chemical , pharmacology : Sulfur Dioxide.
- analysis : Wine.
- Chromatography, Gel, Circular Dichroism, Dynamic Light Scattering, Hydrophobic and Hydrophilic Interactions, Spectrometry, Fluorescence, Temperature.
Abstract
Aggregation of heat unstable wine proteins is responsible for the economically and technologically detrimental problem called wine protein haze. This is caused by the aggregation of thermally unfolded proteins that can precipitate in bottled wine. To study the influence of SO2 in this phenomenon, wine proteins were isolated and thaumatins were identified has the most prone to aggregate in the presence of this compound. Isolated wine thaumatins aggregation was followed by dynamic light scattering (DLS), circular dichroism (CD), fluorescence spectroscopy and size exclusion chromatography (SEC). Our experimental results demonstrate that protein thermal unfolding after exposure of the protein to 70 °C does not present differences whether SO2 is present or not. Conversely, when the protein solution is cooled to 15 °C (after heat stress) significant analytical changes can be observed between samples with and without SO2. A remarkable change of circular dichroism spectra in the region 220-230 nm is observed (which can be related to S-S torsion angles), as well as an increase in tryptophan fluorescence intensity (absence of fluorescence quenching by S-S bonds). Formation of covalently-linked dimeric and tetrameric protein species were also detected by SEC. The ability to dissolve the aggregates with 8 M urea seems to indicate that hydrophobic interactions are prevalent in the formed aggregates. Also, the reduction of these aggregates with tris (2-carboxyethyl) phosphine (TCEP) to only monomeric species reveals the presence of intermolecular S-S bonds.
DOI: 10.1016/j.foodchem.2018.03.115
PubMed: 29680039
Affiliations:
Links toward previous steps (curation, corpus...)
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Laia</name><affiliation wicri:level="1"><nlm:affiliation>LAQV-REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>LAQV-REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Campus de Caparica, 2829-516 Caparica</wicri:regionArea><wicri:noRegion>2829-516 Caparica</wicri:noRegion></affiliation></author><author><name sortKey="Ferreira, Ricardo B" sort="Ferreira, Ricardo B" uniqKey="Ferreira R" first="Ricardo B" last="Ferreira">Ricardo B. 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Electronic address: lpf@fct.unl.pt.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>LAQV-REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Campus de Caparica, 2829-516 Caparica</wicri:regionArea><wicri:noRegion>2829-516 Caparica</wicri:noRegion></affiliation></author></analytic><series><title level="j">Food chemistry</title><idno type="eISSN">1873-7072</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Gel (MeSH)</term><term>Circular Dichroism (MeSH)</term><term>Disulfides (chemistry)</term><term>Dynamic Light Scattering (MeSH)</term><term>Hydrophobic and Hydrophilic Interactions (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (isolation & purification)</term><term>Plant Proteins (metabolism)</term><term>Protein Aggregates (drug effects)</term><term>Spectrometry, Fluorescence (MeSH)</term><term>Sulfur Dioxide (chemistry)</term><term>Sulfur Dioxide (pharmacology)</term><term>Temperature (MeSH)</term><term>Wine (analysis)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agrégats de protéines (effets des médicaments et des substances chimiques)</term><term>Chromatographie sur gel (MeSH)</term><term>Dichroïsme circulaire (MeSH)</term><term>Diffusion dynamique de la lumière (MeSH)</term><term>Dioxyde de soufre (composition chimique)</term><term>Dioxyde de soufre (pharmacologie)</term><term>Disulfures (composition chimique)</term><term>Interactions hydrophobes et hydrophiles (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (isolement et purification)</term><term>Protéines végétales (métabolisme)</term><term>Spectrométrie de fluorescence (MeSH)</term><term>Température (MeSH)</term><term>Vin (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Plant Proteins</term><term>Sulfur Dioxide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Protein Aggregates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" 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" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sulfur Dioxide</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>Dioxyde de soufre</term><term>Disulfures</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Agrégats de protéines</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Dioxyde de soufre</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term><term>Circular Dichroism</term><term>Dynamic Light Scattering</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Spectrometry, Fluorescence</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie sur gel</term><term>Dichroïsme circulaire</term><term>Diffusion dynamique de la lumière</term><term>Interactions hydrophobes et hydrophiles</term><term>Spectrométrie de fluorescence</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Aggregation of heat unstable wine proteins is responsible for the economically and technologically detrimental problem called wine protein haze. This is caused by the aggregation of thermally unfolded proteins that can precipitate in bottled wine. To study the influence of SO<sub>2</sub> in this phenomenon, wine proteins were isolated and thaumatins were identified has the most prone to aggregate in the presence of this compound. Isolated wine thaumatins aggregation was followed by dynamic light scattering (DLS), circular dichroism (CD), fluorescence spectroscopy and size exclusion chromatography (SEC). Our experimental results demonstrate that protein thermal unfolding after exposure of the protein to 70 °C does not present differences whether SO<sub>2</sub> is present or not. Conversely, when the protein solution is cooled to 15 °C (after heat stress) significant analytical changes can be observed between samples with and without SO<sub>2</sub>. A remarkable change of circular dichroism spectra in the region 220-230 nm is observed (which can be related to S-S torsion angles), as well as an increase in tryptophan fluorescence intensity (absence of fluorescence quenching by S-S bonds). Formation of covalently-linked dimeric and tetrameric protein species were also detected by SEC. The ability to dissolve the aggregates with 8 M urea seems to indicate that hydrophobic interactions are prevalent in the formed aggregates. Also, the reduction of these aggregates with tris (2-carboxyethyl) phosphine (TCEP) to only monomeric species reveals the presence of intermolecular S-S bonds.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">29680039</PMID><DateCompleted><Year>2018</Year><Month>10</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-7072</ISSN><JournalIssue CitedMedium="Internet"><Volume>259</Volume><PubDate><Year>2018</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Food chemistry</Title><ISOAbbreviation>Food Chem</ISOAbbreviation></Journal><ArticleTitle>Sulfur dioxide induced aggregation of wine thaumatin-like proteins: Role of disulfide bonds.</ArticleTitle><Pagination><MedlinePgn>166-174</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0308-8146(18)30557-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.foodchem.2018.03.115</ELocationID><Abstract><AbstractText>Aggregation of heat unstable wine proteins is responsible for the economically and technologically detrimental problem called wine protein haze. This is caused by the aggregation of thermally unfolded proteins that can precipitate in bottled wine. To study the influence of SO<sub>2</sub> in this phenomenon, wine proteins were isolated and thaumatins were identified has the most prone to aggregate in the presence of this compound. Isolated wine thaumatins aggregation was followed by dynamic light scattering (DLS), circular dichroism (CD), fluorescence spectroscopy and size exclusion chromatography (SEC). Our experimental results demonstrate that protein thermal unfolding after exposure of the protein to 70 °C does not present differences whether SO<sub>2</sub> is present or not. Conversely, when the protein solution is cooled to 15 °C (after heat stress) significant analytical changes can be observed between samples with and without SO<sub>2</sub>. A remarkable change of circular dichroism spectra in the region 220-230 nm is observed (which can be related to S-S torsion angles), as well as an increase in tryptophan fluorescence intensity (absence of fluorescence quenching by S-S bonds). Formation of covalently-linked dimeric and tetrameric protein species were also detected by SEC. The ability to dissolve the aggregates with 8 M urea seems to indicate that hydrophobic interactions are prevalent in the formed aggregates. Also, the reduction of these aggregates with tris (2-carboxyethyl) phosphine (TCEP) to only monomeric species reveals the presence of intermolecular S-S bonds.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chagas</LastName><ForeName>Ricardo</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>LAQV-REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal; LEAF, Instituto Superior de Agronomia, Universidade de Lisboa, 1349-017 Lisboa, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Laia</LastName><ForeName>César A T</ForeName><Initials>CAT</Initials><AffiliationInfo><Affiliation>LAQV-REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferreira</LastName><ForeName>Ricardo B</ForeName><Initials>RB</Initials><AffiliationInfo><Affiliation>LEAF, Instituto Superior de Agronomia, Universidade de Lisboa, 1349-017 Lisboa, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferreira</LastName><ForeName>Luísa M</ForeName><Initials>LM</Initials><AffiliationInfo><Affiliation>LAQV-REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal. Electronic address: lpf@fct.unl.pt.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>03</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Food Chem</MedlineTA><NlmUniqueID>7702639</NlmUniqueID><ISSNLinking>0308-8146</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D066329">Protein Aggregates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0UZA3422Q4</RegistryNumber><NameOfSubstance UI="D013458">Sulfur Dioxide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000067493" MajorTopicYN="N">Dynamic Light Scattering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057927" MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D066329" MajorTopicYN="N">Protein Aggregates</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013458" MajorTopicYN="N">Sulfur Dioxide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014920" MajorTopicYN="N">Wine</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Haze</Keyword><Keyword MajorTopicYN="N">Protein aggregation</Keyword><Keyword MajorTopicYN="N">Sulfur dioxide</Keyword><Keyword MajorTopicYN="N">Wine</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>12</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>03</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>03</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>4</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>4</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>10</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29680039</ArticleId><ArticleId IdType="pii">S0308-8146(18)30557-0</ArticleId><ArticleId IdType="doi">10.1016/j.foodchem.2018.03.115</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Portugal</li></country></list><tree><country name="Portugal"><noRegion><name sortKey="Chagas, Ricardo" sort="Chagas, Ricardo" uniqKey="Chagas R" first="Ricardo" last="Chagas">Ricardo Chagas</name></noRegion><name sortKey="Ferreira, Luisa M" sort="Ferreira, Luisa M" uniqKey="Ferreira L" first="Luísa M" last="Ferreira">Luísa M. Ferreira</name><name sortKey="Ferreira, Ricardo B" sort="Ferreira, Ricardo B" uniqKey="Ferreira R" first="Ricardo B" last="Ferreira">Ricardo B. Ferreira</name><name sortKey="Laia, Cesar A T" sort="Laia, Cesar A T" uniqKey="Laia C" first="César A T" last="Laia">César A T. Laia</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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