1 Ocak 2018 Dergi makalesi Açık Erişim

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

Dublin Core

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  <dc:creator>Kilic-Akyilmaz, Meral</dc:creator>
  <dc:creator>Kocaman, Esra</dc:creator>
  <dc:creator>Gulsunoglu, Zehra</dc:creator>
  <dc:creator>Sagdic-Oztan, Ceren</dc:creator>
  <dc:creator>Mavazekhan, Solmaz Mohammadipour</dc:creator>
  <dc:date>2018-01-01</dc:date>
  <dc:description>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'&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.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/32883</dc:identifier>
  <dc:identifier>oai:zenodo.org:32883</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>INTERNATIONAL DAIRY JOURNAL 84 85-91</dc:source>
  <dc:title>Changes in physicochemical properties and gelation behaviour of caseinomacropeptide isolate by treatment with transglutaminase</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
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