Dergi makalesi Açık Erişim
Kilic-Akyilmaz, Meral; Kocaman, Esra; Gulsunoglu, Zehra; Sagdic-Oztan, Ceren; Mavazekhan, Solmaz Mohammadipour
<?xml version='1.0' encoding='utf-8'?> <resource xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns="http://datacite.org/schema/kernel-4" xsi:schemaLocation="http://datacite.org/schema/kernel-4 http://schema.datacite.org/meta/kernel-4.1/metadata.xsd"> <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'&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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