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Article Dans Une Revue Journal of Agricultural and Food Chemistry Année : 2003

Formation of soluble and micelle-bound protein aggregates in heated milk

Fanny Guyomarc'H
Andrew J R Law
  • Fonction : Auteur

Résumé

The formation of heat-induced aggregates of kappa-casein and denatured whey proteins was investigated in milk-based dairy mixtures containing casein micelles and serum proteins in different ratios. Both soluble and micelle-bound aggregates were isolated from the mixtures heated at 95 degrees C for 10 min, using size exclusion chromatography. Quantitative analysis of the protein composition of the aggregates by reverse phase high-performance liquid chromatography strongly suggested that primary aggregates of beta-lactoglobulin and alpha-lactalbumin in a 3 to 1 ratio were involved as well as kappa-casein, and alpha(s2)-casein in micellar aggregates. The results gave evidence that heat-induced dissociation of micellar kappa-casein was implicated in the formation of the soluble aggregates and indicated that a significant amount of kappa-casein was left unreacted after heating. The average size of the aggregates was 3.5-5.5 million Da, depending on the available kappa-casein or the casein:whey protein ratio in the mixtures. The size and density of these aggregates relative to those of casein micelles were discussed.

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Dates et versions

hal-00294392 , version 1 (21-07-2008)

Identifiants

  • HAL Id : hal-00294392 , version 1
  • PUBMED : 14705892

Citer

Fanny Guyomarc'H, Andrew J R Law, Douglas G Dalgleish. Formation of soluble and micelle-bound protein aggregates in heated milk. Journal of Agricultural and Food Chemistry, 2003. ⟨hal-00294392⟩
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