Quantification of chitinase and thaumatin-like proteins in grape juices and wines.
Identifieur interne : 000260 ( Main/Corpus ); précédent : 000259; suivant : 000261Quantification of chitinase and thaumatin-like proteins in grape juices and wines.
Auteurs : D. Le Bourse ; A. Conreux ; S. Villaume ; P. Lameiras ; J-M Nuzillard ; P. JeandetSource :
- Analytical and bioanalytical chemistry [ 1618-2650 ] ; 2011.
English descriptors
- KwdEn :
- MESH :
- chemical , isolation & purification : Chitinases, Plant Proteins.
- analysis : Beverages, Wine.
- chemistry : Vitis.
- Chromatography, High Pressure Liquid, Enzyme-Linked Immunosorbent Assay, Nuclear Magnetic Resonance, Biomolecular.
Abstract
Chitinases and thaumatin-like proteins are important grape proteins as they have a great influence on wine quality. The quantification of these proteins in grape juices and wines, along with their purification, is therefore crucial to study their intrinsic characteristics and the exact role they play in wines. The main isoforms of these two proteins from Chardonnay grape juice were thus purified by liquid chromatography. Two fast protein liquid chromatography (FLPC) steps allowed the fractionation and purification of the juice proteins, using cation exchange and hydrophobic interaction media. A further high-performance liquid chromatography (HPLC) step was used to achieve higher purity levels. Fraction assessment was achieved by mass spectrometry. Fraction purity was determined by HPLC to detect the presence of protein contaminants, and by nuclear magnetic resonance (NMR) spectroscopy to detect the presence of organic contaminants. Once pure fractions of lyophilized chitinase and thaumatin-like protein were obtained, ultra-HPLC (UHPLC) and enzyme-linked immunosorbent assay (ELISA) calibration curves were constructed. The quantification of these proteins in different grape juice and wine samples was thus achieved for the first time with both techniques through comparison with the purified protein calibration curve. UHPLC and ELISA showed very consistent results (less than 16% deviation for both proteins) and either could be considered to provide an accurate and reliable quantification of proteins in the oenology field.
DOI: 10.1007/s00216-011-4912-8
PubMed: 21465097
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pubmed:21465097Le document en format XML
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Lameiras</name></author><author><name sortKey="Nuzillard, J M" sort="Nuzillard, J M" uniqKey="Nuzillard J" first="J-M" last="Nuzillard">J-M Nuzillard</name></author><author><name sortKey="Jeandet, P" sort="Jeandet, P" uniqKey="Jeandet P" first="P" last="Jeandet">P. Jeandet</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21465097</idno><idno type="pmid">21465097</idno><idno type="doi">10.1007/s00216-011-4912-8</idno><idno type="wicri:Area/Main/Corpus">000260</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000260</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Quantification of chitinase and thaumatin-like proteins in grape juices and wines.</title><author><name sortKey="Le Bourse, D" sort="Le Bourse, D" uniqKey="Le Bourse D" first="D" last="Le Bourse">D. Le Bourse</name><affiliation><nlm:affiliation>Laboratoire d'Oenologie et Chimie Appliquée, Université de Reims Champagne-Ardenne, URVVC-SE UPRES EA 2069, BP 1039, 51687 Reims Cedex 2, France. doriane.le-bourse@univ-reims.fr</nlm:affiliation></affiliation></author><author><name sortKey="Conreux, A" sort="Conreux, A" uniqKey="Conreux A" first="A" last="Conreux">A. Conreux</name></author><author><name sortKey="Villaume, S" sort="Villaume, S" uniqKey="Villaume S" first="S" last="Villaume">S. Villaume</name></author><author><name sortKey="Lameiras, P" sort="Lameiras, P" uniqKey="Lameiras P" first="P" last="Lameiras">P. Lameiras</name></author><author><name sortKey="Nuzillard, J M" sort="Nuzillard, J M" uniqKey="Nuzillard J" first="J-M" last="Nuzillard">J-M Nuzillard</name></author><author><name sortKey="Jeandet, P" sort="Jeandet, P" uniqKey="Jeandet P" first="P" last="Jeandet">P. Jeandet</name></author></analytic><series><title level="j">Analytical and bioanalytical chemistry</title><idno type="eISSN">1618-2650</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Beverages (analysis)</term><term>Chitinases (isolation & purification)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Enzyme-Linked Immunosorbent Assay (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term><term>Plant Proteins (isolation & purification)</term><term>Vitis (chemistry)</term><term>Wine (analysis)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Chitinases</term><term>Plant Proteins</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" xml:lang="en"><term>Chromatography, High Pressure Liquid</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Nuclear Magnetic Resonance, Biomolecular</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Chitinases and thaumatin-like proteins are important grape proteins as they have a great influence on wine quality. The quantification of these proteins in grape juices and wines, along with their purification, is therefore crucial to study their intrinsic characteristics and the exact role they play in wines. The main isoforms of these two proteins from Chardonnay grape juice were thus purified by liquid chromatography. Two fast protein liquid chromatography (FLPC) steps allowed the fractionation and purification of the juice proteins, using cation exchange and hydrophobic interaction media. A further high-performance liquid chromatography (HPLC) step was used to achieve higher purity levels. Fraction assessment was achieved by mass spectrometry. Fraction purity was determined by HPLC to detect the presence of protein contaminants, and by nuclear magnetic resonance (NMR) spectroscopy to detect the presence of organic contaminants. Once pure fractions of lyophilized chitinase and thaumatin-like protein were obtained, ultra-HPLC (UHPLC) and enzyme-linked immunosorbent assay (ELISA) calibration curves were constructed. The quantification of these proteins in different grape juice and wine samples was thus achieved for the first time with both techniques through comparison with the purified protein calibration curve. UHPLC and ELISA showed very consistent results (less than 16% deviation for both proteins) and either could be considered to provide an accurate and reliable quantification of proteins in the oenology field.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21465097</PMID><DateCompleted><Year>2011</Year><Month>12</Month><Day>09</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1618-2650</ISSN><JournalIssue CitedMedium="Internet"><Volume>401</Volume><Issue>5</Issue><PubDate><Year>2011</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Analytical and bioanalytical chemistry</Title><ISOAbbreviation>Anal Bioanal Chem</ISOAbbreviation></Journal><ArticleTitle>Quantification of chitinase and thaumatin-like proteins in grape juices and wines.</ArticleTitle><Pagination><MedlinePgn>1541-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00216-011-4912-8</ELocationID><Abstract><AbstractText>Chitinases and thaumatin-like proteins are important grape proteins as they have a great influence on wine quality. The quantification of these proteins in grape juices and wines, along with their purification, is therefore crucial to study their intrinsic characteristics and the exact role they play in wines. The main isoforms of these two proteins from Chardonnay grape juice were thus purified by liquid chromatography. Two fast protein liquid chromatography (FLPC) steps allowed the fractionation and purification of the juice proteins, using cation exchange and hydrophobic interaction media. A further high-performance liquid chromatography (HPLC) step was used to achieve higher purity levels. Fraction assessment was achieved by mass spectrometry. Fraction purity was determined by HPLC to detect the presence of protein contaminants, and by nuclear magnetic resonance (NMR) spectroscopy to detect the presence of organic contaminants. Once pure fractions of lyophilized chitinase and thaumatin-like protein were obtained, ultra-HPLC (UHPLC) and enzyme-linked immunosorbent assay (ELISA) calibration curves were constructed. The quantification of these proteins in different grape juice and wine samples was thus achieved for the first time with both techniques through comparison with the purified protein calibration curve. UHPLC and ELISA showed very consistent results (less than 16% deviation for both proteins) and either could be considered to provide an accurate and reliable quantification of proteins in the oenology field.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Le Bourse</LastName><ForeName>D</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Laboratoire d'Oenologie et Chimie Appliquée, Université de Reims Champagne-Ardenne, URVVC-SE UPRES EA 2069, BP 1039, 51687 Reims Cedex 2, France. doriane.le-bourse@univ-reims.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Conreux</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Villaume</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Lameiras</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Nuzillard</LastName><ForeName>J-M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Jeandet</LastName><ForeName>P</ForeName><Initials>P</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><ArticleDate DateType="Electronic"><Year>2011</Year><Month>04</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Anal Bioanal Chem</MedlineTA><NlmUniqueID>101134327</NlmUniqueID><ISSNLinking>1618-2642</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.14</RegistryNumber><NameOfSubstance UI="D002688">Chitinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Anal Bioanal Chem. 2011 Sep;401(5):1713</RefSource></CommentsCorrections></CommentsCorrectionsList><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="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D027843" MajorTopicYN="N">Vitis</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014920" MajorTopicYN="N">Wine</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>02</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>03</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2011</Year><Month>03</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>4</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>4</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>12</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21465097</ArticleId><ArticleId IdType="doi">10.1007/s00216-011-4912-8</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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