Proteomic profiling of camel and cow milk proteins under heat treatment.
Identifieur interne : 000347 ( Main/Merge ); précédent : 000346; suivant : 000348Proteomic profiling of camel and cow milk proteins under heat treatment.
Auteurs : Imène Felfoul [Tunisie] ; Julien Jardin [France] ; Frédéric Gaucheron [France] ; Hamadi Attia [Tunisie] ; M A Ayadi [Tunisie]Source :
- Food chemistry [ 1873-7072 ] ; 2017.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Caséines (analyse), Chameaux (MeSH), Chromatographie en phase liquide (MeSH), Lactoglobulines (analyse), Protéines de lactosérum (analyse), Protéines de lactosérum (composition chimique), Protéines de lait (analyse), Protéomique (MeSH), Spectrométrie de masse en tandem (MeSH), Température élevée (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
English descriptors
- KwdEn :
- Animals (MeSH), Camelus (MeSH), Caseins (analysis), Cattle (MeSH), Chromatography, Liquid (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Hot Temperature (MeSH), Lactoglobulins (analysis), Milk Proteins (analysis), Proteomics (MeSH), Tandem Mass Spectrometry (MeSH), Whey Proteins (analysis), Whey Proteins (chemistry).
- MESH :
- chemical , analysis : Caseins, Lactoglobulins, Milk Proteins, Whey Proteins.
- chemical , chemistry : Whey Proteins.
- Animals, Camelus, Cattle, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Hot Temperature, Proteomics, Tandem Mass Spectrometry.
Abstract
Cow and camel milk proteins before and after heat treatment at 80°C for 60min were identified using LC/MS and LC-MS/MS following monodimensional electrophoresis. The database used for the identification of camel and cow proteins was set from http://www.uniprot.org/. The obtained results showed that, after heating, camel milk at 80°C for 60min, camel α-lactalbumin (α-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA) was significantly diminished. When heating cow milk at 80°C for 60min, α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were not significantly detected. Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins were identified by LC-MS/MS. Casein fractions were kept intact under a heat treatment of 80°C during 60min of both camel and cow milks. Camel and bovine whey proteins were affected by a heat treatment of 80°C for 60min.
DOI: 10.1016/j.foodchem.2016.08.007
PubMed: 27596405
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Electronic address: ayadimedali@yahoo.fr.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038</wicri:regionArea><wicri:noRegion>Sfax 3038</wicri:noRegion></affiliation></author></analytic><series><title level="j">Food chemistry</title><idno type="eISSN">1873-7072</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Camelus (MeSH)</term><term>Caseins (analysis)</term><term>Cattle (MeSH)</term><term>Chromatography, Liquid (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Hot Temperature (MeSH)</term><term>Lactoglobulins (analysis)</term><term>Milk Proteins (analysis)</term><term>Proteomics (MeSH)</term><term>Tandem Mass Spectrometry (MeSH)</term><term>Whey Proteins (analysis)</term><term>Whey Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Caséines (analyse)</term><term>Chameaux (MeSH)</term><term>Chromatographie en phase liquide (MeSH)</term><term>Lactoglobulines (analyse)</term><term>Protéines de lactosérum (analyse)</term><term>Protéines de lactosérum (composition chimique)</term><term>Protéines de lait (analyse)</term><term>Protéomique (MeSH)</term><term>Spectrométrie de masse en tandem (MeSH)</term><term>Température élevée (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Caseins</term><term>Lactoglobulins</term><term>Milk Proteins</term><term>Whey Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Whey Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Caséines</term><term>Lactoglobulines</term><term>Protéines de lactosérum</term><term>Protéines de lait</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines de lactosérum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Camelus</term><term>Cattle</term><term>Chromatography, Liquid</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Hot Temperature</term><term>Proteomics</term><term>Tandem Mass Spectrometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Chameaux</term><term>Chromatographie en phase liquide</term><term>Protéomique</term><term>Spectrométrie de masse en tandem</term><term>Température élevée</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cow and camel milk proteins before and after heat treatment at 80°C for 60min were identified using LC/MS and LC-MS/MS following monodimensional electrophoresis. The database used for the identification of camel and cow proteins was set from http://www.uniprot.org/. The obtained results showed that, after heating, camel milk at 80°C for 60min, camel α-lactalbumin (α-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA) was significantly diminished. When heating cow milk at 80°C for 60min, α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were not significantly detected. Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins were identified by LC-MS/MS. Casein fractions were kept intact under a heat treatment of 80°C during 60min of both camel and cow milks. Camel and bovine whey proteins were affected by a heat treatment of 80°C for 60min. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">27596405</PMID><DateCompleted><Year>2016</Year><Month>12</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-7072</ISSN><JournalIssue CitedMedium="Internet"><Volume>216</Volume><PubDate><Year>2017</Year><Month>Feb</Month><Day>01</Day></PubDate></JournalIssue><Title>Food chemistry</Title><ISOAbbreviation>Food Chem</ISOAbbreviation></Journal><ArticleTitle>Proteomic profiling of camel and cow milk proteins under heat treatment.</ArticleTitle><Pagination><MedlinePgn>161-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.foodchem.2016.08.007</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0308-8146(16)31237-7</ELocationID><Abstract><AbstractText>Cow and camel milk proteins before and after heat treatment at 80°C for 60min were identified using LC/MS and LC-MS/MS following monodimensional electrophoresis. The database used for the identification of camel and cow proteins was set from http://www.uniprot.org/. The obtained results showed that, after heating, camel milk at 80°C for 60min, camel α-lactalbumin (α-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA) was significantly diminished. When heating cow milk at 80°C for 60min, α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were not significantly detected. Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins were identified by LC-MS/MS. Casein fractions were kept intact under a heat treatment of 80°C during 60min of both camel and cow milks. Camel and bovine whey proteins were affected by a heat treatment of 80°C for 60min. </AbstractText><CopyrightInformation>Copyright © 2016 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Felfoul</LastName><ForeName>Imène</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jardin</LastName><ForeName>Julien</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>INRA, UMR1253 STLO, 65 rue de Saint-Brieuc, F-35000 Rennes, France; Agrocampus Ouest, UMR 1253 STLO, 65 rue de Saint Brieuc, F-35000, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gaucheron</LastName><ForeName>Frédéric</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>INRA, UMR1253 STLO, 65 rue de Saint-Brieuc, F-35000 Rennes, France; Agrocampus Ouest, UMR 1253 STLO, 65 rue de Saint Brieuc, F-35000, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Attia</LastName><ForeName>Hamadi</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ayadi</LastName><ForeName>M A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038, Tunisia. Electronic address: ayadimedali@yahoo.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>08</Month><Day>04</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="D002364">Caseins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007782">Lactoglobulins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008894">Milk Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000067816">Whey Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002162" MajorTopicYN="N">Camelus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002364" MajorTopicYN="N">Caseins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002853" MajorTopicYN="N">Chromatography, Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007782" MajorTopicYN="N">Lactoglobulins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008894" MajorTopicYN="N">Milk Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="Y">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053719" MajorTopicYN="N">Tandem Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000067816" MajorTopicYN="N">Whey Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Camel milk</Keyword><Keyword MajorTopicYN="N">Cow milk</Keyword><Keyword MajorTopicYN="N">Electrophoresis</Keyword><Keyword MajorTopicYN="N">Heat treatment</Keyword><Keyword MajorTopicYN="N">LC/MS</Keyword><Keyword MajorTopicYN="N">LC–MS/MS</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>05</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>08</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>08</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>9</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>9</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27596405</ArticleId><ArticleId IdType="pii">S0308-8146(16)31237-7</ArticleId><ArticleId IdType="doi">10.1016/j.foodchem.2016.08.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li><li>Tunisie</li></country><region><li>Région Bretagne</li></region></list><tree><country name="Tunisie"><noRegion><name sortKey="Felfoul, Imene" sort="Felfoul, Imene" uniqKey="Felfoul I" first="Imène" last="Felfoul">Imène Felfoul</name></noRegion><name sortKey="Attia, Hamadi" sort="Attia, Hamadi" uniqKey="Attia H" first="Hamadi" last="Attia">Hamadi Attia</name><name sortKey="Ayadi, M A" sort="Ayadi, M A" uniqKey="Ayadi M" first="M A" last="Ayadi">M A Ayadi</name></country><country name="France"><region name="Région Bretagne"><name sortKey="Jardin, Julien" sort="Jardin, Julien" uniqKey="Jardin J" first="Julien" last="Jardin">Julien Jardin</name></region><name sortKey="Gaucheron, Frederic" sort="Gaucheron, Frederic" uniqKey="Gaucheron F" first="Frédéric" last="Gaucheron">Frédéric Gaucheron</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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