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Acta AlimentariaVolume 34, Issue 2, June 2005, Pages 105-112

Page analysis of milk proteins altered by high thermal treatment(Article)

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  • Department of Food Science and Biochemistry, Faculty of Agriculture, University of Belgrade, Nemanjina 6, 11080 Zemun, Serbia

Abstract

Changes that occur in milk proteins during heat treatment were studied. Milk was heat treated at 87°C for 10 min. Samples of untreated milk, demineralised whey powder and heat treated milk were analysed by discontinuous PAGE and by densitometric analysis of destained gels. PAGE experiments showed that heat treatment induces changes on milk proteins. During heating at 87°C for 10 min all amount of β-lactoglobulin present in milk interacted with casein, while small amount of α-lactalbumin did not interact with casein. It could be hypothesised that heating of milk at 87°C for 10 min influences complete denaturation of β-lactoglobulin and formation of complex with casein, while α-lactalbumin denatures and interacts with β-lactoglobulin when β-lactoglobulin has already linked with casein micelles. © 2005 Akadémiai Kiadó.

Author keywords

Heat treatmentMilk proteinsPAGE

Indexed keywords

EMTREE drug terms:alpha lactalbuminbeta lactoglobulincaseinmilk protein
EMTREE medical terms:articlecomplex formationdemineralizationfood analysisheat treatmentmicellepolyacrylamide gel electrophoresispowderprotein denaturationprotein protein interactionwhey

Chemicals and CAS Registry Numbers:

alpha lactalbumin, 9051-29-0; beta lactoglobulin, 9045-23-2; casein, 9000-71-9

  • ISSN: 01393006
  • Source Type: Journal
  • Original language: English
  • DOI: 10.1556/AAlim.34.2005.2.2
  • Document Type: Article
  • Publisher: Akademiai Kiado Rt.

  Jovanović, S.; Department of Food Science and Biochemistry, Faculty of Agriculture, University of Belgrade, Nemanjina 6, Serbia;
© Copyright 2019 Elsevier B.V., All rights reserved.

Cited by 7 documents

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View details of all 7 citations
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