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Changes in physicochemical properties and gelation behaviour of caseinomacropeptide isolate by treatment with transglutaminase

Kilic-Akyilmaz, Meral; Kocaman, Esra; Gulsunoglu, Zehra; Sagdic-Oztan, Ceren; Mavazekhan, Solmaz Mohammadipour


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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/32883</identifier>
  <creators>
    <creator>
      <creatorName>Kilic-Akyilmaz, Meral</creatorName>
      <givenName>Meral</givenName>
      <familyName>Kilic-Akyilmaz</familyName>
      <affiliation>Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Kocaman, Esra</creatorName>
      <givenName>Esra</givenName>
      <familyName>Kocaman</familyName>
      <affiliation>Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Gulsunoglu, Zehra</creatorName>
      <givenName>Zehra</givenName>
      <familyName>Gulsunoglu</familyName>
      <affiliation>Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Sagdic-Oztan, Ceren</creatorName>
      <givenName>Ceren</givenName>
      <familyName>Sagdic-Oztan</familyName>
      <affiliation>Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Mavazekhan, Solmaz Mohammadipour</creatorName>
      <givenName>Solmaz Mohammadipour</givenName>
      <familyName>Mavazekhan</familyName>
      <affiliation>Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey</affiliation>
    </creator>
  </creators>
  <titles>
    <title>Changes In Physicochemical Properties And Gelation Behaviour Of Caseinomacropeptide Isolate By Treatment With Transglutaminase</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2018</publicationYear>
  <dates>
    <date dateType="Issued">2018-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/32883</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1016/j.idairyj.2018.04.005</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">The gelation behaviour of caseinomacropeptide isolate (CMPI) treated with transglutaminase at levels of 1 and 25 U g(-1) protein was investigated at different pH and temperatures. Cross-linking of CMPI protein fractions by transglutaminase was confirmed using tricine-sodium dodecylsulphate-polyacrylamide gel electrophoresis. Cross-linking reduced the isoelectric point and hydrophobicity of CMPI. The gelation temperature of CMPI at pH 3 was reduced from 54 to 42 degrees C; a gel point (G'&amp;gt;1 Pa) was not observed at pH 4.5 after enzyme treatment during temperature sweep measurements. Cross-linked CMPI formed a gel with lower stiffness and fracture stress at 90 degrees C at pH 3.0 or 4.5 compared with gels of untreated CMPI. However, stiffness and fracture stress of CMPI gels formed at 70 degrees C at pH 3.0 increased by three-and four-fold, respectively, by cross-linking with 25 U g(-1) protein of enzyme. Transglutaminase affected gelation of CMPI by cross-linking of both CMP and residual whey proteins. (c) 2018 Elsevier Ltd. All rights reserved.</description>
  </descriptions>
</resource>
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