Dergi makalesi Açık Erişim
Kilic-Akyilmaz, Meral; Kocaman, Esra; Gulsunoglu, Zehra; Sagdic-Oztan, Ceren; Mavazekhan, Solmaz Mohammadipour
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"affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey",
"name": "Kilic-Akyilmaz, Meral"
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"affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey",
"name": "Kocaman, Esra"
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"affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey",
"name": "Gulsunoglu, Zehra"
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"affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey",
"name": "Sagdic-Oztan, Ceren"
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"affiliation": "Istanbul Tech Univ, Dept Food Engn, TR-34469 Istanbul, Turkey",
"name": "Mavazekhan, Solmaz Mohammadipour"
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"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.",
"doi": "10.1016/j.idairyj.2018.04.005",
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"pages": "85-91",
"title": "INTERNATIONAL DAIRY JOURNAL",
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"title": "Changes in physicochemical properties and gelation behaviour of caseinomacropeptide isolate by treatment with transglutaminase"
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