1 Ocak 2018 Dergi makalesi Açık Erişim

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

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{
  "@context": "https://schema.org/", 
  "@id": 32883, 
  "@type": "ScholarlyArticle", 
  "creator": [
    {
      "@type": "Person", 
      "affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey", 
      "name": "Kilic-Akyilmaz, Meral"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey", 
      "name": "Kocaman, Esra"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey", 
      "name": "Gulsunoglu, Zehra"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey", 
      "name": "Sagdic-Oztan, Ceren"
    }, 
    {
      "@type": "Person", 
      "affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey", 
      "name": "Mavazekhan, Solmaz Mohammadipour"
    }
  ], 
  "datePublished": "2018-01-01", 
  "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'>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.", 
  "headline": "Changes in physicochemical properties and gelation behaviour of caseinomacropeptide isolate by treatment with transglutaminase", 
  "identifier": 32883, 
  "image": "https://aperta.ulakbim.gov.tr/static/img/logo/aperta_logo_with_icon.svg", 
  "license": "http://www.opendefinition.org/licenses/cc-by", 
  "name": "Changes in physicochemical properties and gelation behaviour of caseinomacropeptide isolate by treatment with transglutaminase", 
  "url": "https://aperta.ulakbim.gov.tr/record/32883"
}