Role of the soluble and micelle-bound heat-induced protein aggregates on network formation in acid skim milk gels.
Gel formation was monitored by low amplitude rheometry during acidification at 40 degrees C with 1.5% glucono-delta-lactone in combined milk systems containing soluble and/or micelle-bound heat-induced (95 degrees C/10 min) aggregates of denatured whey proteins and kappa-casein and in heated dairy mixes with varying micellar casein/whey protein ratio (CN/WP). Both soluble and micelle-bound aggregates increased gelation pH and gel strength. Micelle-bound aggregates seemed to modify the micelle surface so that micelles were destabilized at a pH of 5.1 (instead of 4.7), while soluble aggregates precipitated at their calculated pI of approximately 5.3, and initiated an early gelation by interacting with the micelles. Decreasing the CN/WP ratio produced larger aggregates with higher whey protein: kappa-casein ratio, which gave more elastic gels. The specific effects of the micellar and soluble aggregates on gel strength are discussed with respect to their relative proportions in the heated milk.
Guyomarc'h
Fanny
F
Danone Vitapole Recherche, RD 128, 91 767 Palaiseau, France, and The Hannah Research Park, Ayr KA6 5HL, Scotland, UK. guymmar@labtechno.raozhon.inra.fr
Queguiner
Claire
C
Law
Andrew J R
AJ
Horne
David S
DS
Dalgleish
Douglas G
DG
D000818:Animals; D002364:Caseins / Q000032:analysis / Q000737:chemistry; D004548:Elasticity; D005782:Gels / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008823:Micelles; D008892:Milk / Q000737:chemistry*; D008894:Milk Proteins / Q000032:analysis / Q000737:chemistry*; D012995:Solubility; D014783:Viscosity; D000067816:Whey Proteins
D002364:Caseins; D005782:Gels; D008823:Micelles; D008894:Milk Proteins; D000067816:Whey Proteins