Gelation upon long storage of milk drinks with carrageenan.
The carrageenan-induced stabilization and gelation of ultra-high-temperature-treated milk was studied during long storage. Severe heating (causing increased protein denaturation), lowering of the pH, or the use of kappa-carrageenan (instead of iota-carrageenan) led to excessive gelation. It is suggested that the balance between carrageenan-carrageenan interactions and carrageenan-protein interactions determines the gel strength. If the interactions between carrageenan and proteins are decreased, more carrageenan is available for carrageenan-carrageenan interactions, leading to a stronger gel. This is the case if kappa-carrageenan is used instead of iota-carrageenan because the former forms weaker interactions with proteins than the latter. Also, heating and pH influence the attachment of whey proteins to the casein micelle surface, hindering the attachment of carrageenan to the casein proteins. Upon storage, gel strength increased. Particle size and rheology measurements indicated that upon storage, tenuous carrageenan-protein aggregates are formed. The firming of the gel was probably related to slow structural arrangements of the gel and not related to slowly changing calcium equilibria or age gelation.
Tijssen
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RL
Unilever R&D Vlaardingen, 3130 AC Vlaardingen, The Netherlands. Renske.Tijssen@unilever.com
Canabady-Rochelle
L S
LS
Mellema
M
M
D000818:Animals; D001628:Beverages; D002351:Carrageenan / Q000737:chemistry*; D005519:Food Preservation / Q000379:methods*; D005524:Food Technology; D005782:Gels / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008892:Milk / Q000737:chemistry*; D008894:Milk Proteins / Q000737:chemistry*; D010316:Particle Size; D012212:Rheology; D013997:Time Factors
D005782:Gels; D008894:Milk Proteins; D002351:Carrageenan