Thermal stability of thaumatin-like protein, chitinase, and invertase isolated from Sauvignon blanc and Semillon juice and their role in haze formation in wine.
Identifieur interne : 000276 ( Main/Exploration ); précédent : 000275; suivant : 000277Thermal stability of thaumatin-like protein, chitinase, and invertase isolated from Sauvignon blanc and Semillon juice and their role in haze formation in wine.
Auteurs : Robert J. Falconer [Australie] ; Matteo Marangon ; Steven C. Van Sluyter ; Karlie A. Neilson ; Cherrine Chan ; Elizabeth J. WatersSource :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2010.
Descripteurs français
- KwdFr :
- Boissons (analyse), Chitinase (composition chimique), Chitinase (isolement et purification), Cinétique (MeSH), Conformation des protéines (MeSH), Pliage des protéines (MeSH), Protéines végétales (composition chimique), Protéines végétales (isolement et purification), Stabilité protéique (MeSH), Thermodynamique (MeSH), Vin (analyse), Vitis (composition chimique), Vitis (enzymologie), beta-Fructofuranosidase (composition chimique), beta-Fructofuranosidase (isolement et purification).
- MESH :
- analyse : Boissons, Vin.
- composition chimique : Chitinase, Protéines végétales, Vitis, beta-Fructofuranosidase.
- enzymologie : Vitis.
- isolement et purification : Chitinase, Protéines végétales, beta-Fructofuranosidase.
- Cinétique, Conformation des protéines, Pliage des protéines, Stabilité protéique, Thermodynamique.
English descriptors
- KwdEn :
- Beverages (analysis), Chitinases (chemistry), Chitinases (isolation & purification), Kinetics (MeSH), Plant Proteins (chemistry), Plant Proteins (isolation & purification), Protein Conformation (MeSH), Protein Folding (MeSH), Protein Stability (MeSH), Thermodynamics (MeSH), Vitis (chemistry), Vitis (enzymology), Wine (analysis), beta-Fructofuranosidase (chemistry), beta-Fructofuranosidase (isolation & purification).
- MESH :
- chemical , chemistry : Chitinases, Plant Proteins, beta-Fructofuranosidase.
- analysis : Beverages, Wine.
- chemistry : Vitis.
- enzymology : Vitis.
- chemical , isolation & purification : Chitinases, Plant Proteins, beta-Fructofuranosidase.
- Kinetics, Protein Conformation, Protein Folding, Protein Stability, Thermodynamics.
Abstract
A thermal unfolding study of thaumatin-like protein, chitinase, and invertase isolated from Vitis vinifera Sauvignon blanc and Semillon juice was undertaken. Differential scanning calorimetry demonstrated that chitinase was a major player in heat-induced haze in unfined wines as it had a low melt temperature, and aggregation was observed. The kinetics of chitinase F1 (Sauvignon blanc) unfolding was studied using circular dichroism spectrometry. Chitinase unfolding conforms to Arrhenius behavior having an activation energy of 320 kJ/mol. This enabled a predictive model for protein stability to be generated, predicting a half-life of 9 years at 15 degrees C, 4.7 days at 30 degrees C, and 17 min at 45 degrees C. Circular dichroism studies indicate that chitinase unfolding follows three steps: an initial irreversible step from the native to an unfolded conformation, a reversible step between a collapsed and an unfolded non-native conformation, followed by irreversible aggregation associated with visible haze formation.
DOI: 10.1021/jf902843b
PubMed: 20014848
Affiliations:
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Falconer</name><affiliation wicri:level="1"><nlm:affiliation>Australian Institute for Bioengineering and Nanotechnology, University of Queensland, QLD 4072, Australia. r.falconer@uq.edu.au</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Australian Institute for Bioengineering and Nanotechnology, University of Queensland, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Marangon, Matteo" sort="Marangon, Matteo" uniqKey="Marangon M" first="Matteo" last="Marangon">Matteo Marangon</name></author><author><name sortKey="Van Sluyter, Steven C" sort="Van Sluyter, Steven C" uniqKey="Van Sluyter S" first="Steven C" last="Van Sluyter">Steven C. Van Sluyter</name></author><author><name sortKey="Neilson, Karlie A" sort="Neilson, Karlie A" uniqKey="Neilson K" first="Karlie A" last="Neilson">Karlie A. Neilson</name></author><author><name sortKey="Chan, Cherrine" sort="Chan, Cherrine" uniqKey="Chan C" first="Cherrine" last="Chan">Cherrine Chan</name></author><author><name sortKey="Waters, Elizabeth J" sort="Waters, Elizabeth J" uniqKey="Waters E" first="Elizabeth J" last="Waters">Elizabeth J. 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Falconer</name><affiliation wicri:level="1"><nlm:affiliation>Australian Institute for Bioengineering and Nanotechnology, University of Queensland, QLD 4072, Australia. r.falconer@uq.edu.au</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Australian Institute for Bioengineering and Nanotechnology, University of Queensland, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Marangon, Matteo" sort="Marangon, Matteo" uniqKey="Marangon M" first="Matteo" last="Marangon">Matteo Marangon</name></author><author><name sortKey="Van Sluyter, Steven C" sort="Van Sluyter, Steven C" uniqKey="Van Sluyter S" first="Steven C" last="Van Sluyter">Steven C. Van Sluyter</name></author><author><name sortKey="Neilson, Karlie A" sort="Neilson, Karlie A" uniqKey="Neilson K" first="Karlie A" last="Neilson">Karlie A. Neilson</name></author><author><name sortKey="Chan, Cherrine" sort="Chan, Cherrine" uniqKey="Chan C" first="Cherrine" last="Chan">Cherrine Chan</name></author><author><name sortKey="Waters, Elizabeth J" sort="Waters, Elizabeth J" uniqKey="Waters E" first="Elizabeth J" last="Waters">Elizabeth J. Waters</name></author></analytic><series><title level="j">Journal of agricultural and food chemistry</title><idno type="eISSN">1520-5118</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Beverages (analysis)</term><term>Chitinases (chemistry)</term><term>Chitinases (isolation & purification)</term><term>Kinetics (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (isolation & purification)</term><term>Protein Conformation (MeSH)</term><term>Protein Folding (MeSH)</term><term>Protein Stability (MeSH)</term><term>Thermodynamics (MeSH)</term><term>Vitis (chemistry)</term><term>Vitis (enzymology)</term><term>Wine (analysis)</term><term>beta-Fructofuranosidase (chemistry)</term><term>beta-Fructofuranosidase (isolation & purification)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Boissons (analyse)</term><term>Chitinase (composition chimique)</term><term>Chitinase (isolement et purification)</term><term>Cinétique (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Pliage des protéines (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (isolement et purification)</term><term>Stabilité protéique (MeSH)</term><term>Thermodynamique (MeSH)</term><term>Vin (analyse)</term><term>Vitis (composition chimique)</term><term>Vitis (enzymologie)</term><term>beta-Fructofuranosidase (composition chimique)</term><term>beta-Fructofuranosidase (isolement et purification)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chitinases</term><term>Plant Proteins</term><term>beta-Fructofuranosidase</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Boissons</term><term>Vin</term></keywords><keywords scheme="MESH" qualifier="analysis" xml:lang="en"><term>Beverages</term><term>Wine</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Chitinase</term><term>Protéines végétales</term><term>Vitis</term><term>beta-Fructofuranosidase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Vitis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Vitis</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Chitinases</term><term>Plant Proteins</term><term>beta-Fructofuranosidase</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Chitinase</term><term>Protéines végétales</term><term>beta-Fructofuranosidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Kinetics</term><term>Protein Conformation</term><term>Protein Folding</term><term>Protein Stability</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Conformation des protéines</term><term>Pliage des protéines</term><term>Stabilité protéique</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A thermal unfolding study of thaumatin-like protein, chitinase, and invertase isolated from Vitis vinifera Sauvignon blanc and Semillon juice was undertaken. Differential scanning calorimetry demonstrated that chitinase was a major player in heat-induced haze in unfined wines as it had a low melt temperature, and aggregation was observed. The kinetics of chitinase F1 (Sauvignon blanc) unfolding was studied using circular dichroism spectrometry. Chitinase unfolding conforms to Arrhenius behavior having an activation energy of 320 kJ/mol. This enabled a predictive model for protein stability to be generated, predicting a half-life of 9 years at 15 degrees C, 4.7 days at 30 degrees C, and 17 min at 45 degrees C. Circular dichroism studies indicate that chitinase unfolding follows three steps: an initial irreversible step from the native to an unfolded conformation, a reversible step between a collapsed and an unfolded non-native conformation, followed by irreversible aggregation associated with visible haze formation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20014848</PMID><DateCompleted><Year>2010</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1520-5118</ISSN><JournalIssue CitedMedium="Internet"><Volume>58</Volume><Issue>2</Issue><PubDate><Year>2010</Year><Month>Jan</Month><Day>27</Day></PubDate></JournalIssue><Title>Journal of agricultural and food chemistry</Title><ISOAbbreviation>J Agric Food Chem</ISOAbbreviation></Journal><ArticleTitle>Thermal stability of thaumatin-like protein, chitinase, and invertase isolated from Sauvignon blanc and Semillon juice and their role in haze formation in wine.</ArticleTitle><Pagination><MedlinePgn>975-80</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jf902843b</ELocationID><Abstract><AbstractText>A thermal unfolding study of thaumatin-like protein, chitinase, and invertase isolated from Vitis vinifera Sauvignon blanc and Semillon juice was undertaken. Differential scanning calorimetry demonstrated that chitinase was a major player in heat-induced haze in unfined wines as it had a low melt temperature, and aggregation was observed. The kinetics of chitinase F1 (Sauvignon blanc) unfolding was studied using circular dichroism spectrometry. Chitinase unfolding conforms to Arrhenius behavior having an activation energy of 320 kJ/mol. This enabled a predictive model for protein stability to be generated, predicting a half-life of 9 years at 15 degrees C, 4.7 days at 30 degrees C, and 17 min at 45 degrees C. Circular dichroism studies indicate that chitinase unfolding follows three steps: an initial irreversible step from the native to an unfolded conformation, a reversible step between a collapsed and an unfolded non-native conformation, followed by irreversible aggregation associated with visible haze formation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Falconer</LastName><ForeName>Robert J</ForeName><Initials>RJ</Initials><AffiliationInfo><Affiliation>Australian Institute for Bioengineering and Nanotechnology, University of Queensland, QLD 4072, Australia. r.falconer@uq.edu.au</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Marangon</LastName><ForeName>Matteo</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Van Sluyter</LastName><ForeName>Steven C</ForeName><Initials>SC</Initials></Author><Author ValidYN="Y"><LastName>Neilson</LastName><ForeName>Karlie A</ForeName><Initials>KA</Initials></Author><Author ValidYN="Y"><LastName>Chan</LastName><ForeName>Cherrine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Waters</LastName><ForeName>Elizabeth J</ForeName><Initials>EJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Agric Food Chem</MedlineTA><NlmUniqueID>0374755</NlmUniqueID><ISSNLinking>0021-8561</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.14</RegistryNumber><NameOfSubstance UI="D002688">Chitinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.26</RegistryNumber><NameOfSubstance UI="D043324">beta-Fructofuranosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001628" MajorTopicYN="N">Beverages</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002688" MajorTopicYN="N">Chitinases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</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></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D027843" MajorTopicYN="N">Vitis</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014920" MajorTopicYN="N">Wine</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043324" MajorTopicYN="N">beta-Fructofuranosidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>3</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20014848</ArticleId><ArticleId IdType="doi">10.1021/jf902843b</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country></list><tree><noCountry><name sortKey="Chan, Cherrine" sort="Chan, Cherrine" uniqKey="Chan C" first="Cherrine" last="Chan">Cherrine Chan</name><name sortKey="Marangon, Matteo" sort="Marangon, Matteo" uniqKey="Marangon M" first="Matteo" last="Marangon">Matteo Marangon</name><name sortKey="Neilson, Karlie A" sort="Neilson, Karlie A" uniqKey="Neilson K" first="Karlie A" last="Neilson">Karlie A. Neilson</name><name sortKey="Van Sluyter, Steven C" sort="Van Sluyter, Steven C" uniqKey="Van Sluyter S" first="Steven C" last="Van Sluyter">Steven C. Van Sluyter</name><name sortKey="Waters, Elizabeth J" sort="Waters, Elizabeth J" uniqKey="Waters E" first="Elizabeth J" last="Waters">Elizabeth J. Waters</name></noCountry><country name="Australie"><noRegion><name sortKey="Falconer, Robert J" sort="Falconer, Robert J" uniqKey="Falconer R" first="Robert J" last="Falconer">Robert J. Falconer</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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