2014
DOI: 10.1016/j.foodhyd.2013.10.004
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Effect of carrageenan on the formation of rennet-induced casein micelle gels

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Cited by 24 publications
(18 citation statements)
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“…It was still unclear that carrageenan affected cheese quality by increasing the moisture content or by interrupting the interactions between casein molecules. Our previous study (Wang and others ) showed that κ‐carrageenan, ι‐carrageenan, and λ‐carrageenan adsorb onto the surface of casein in different ways at low concentrations (for example, tail adsorption, flat adsorption, and ring adsorption for 0.2 g/kg κ‐carrageenan, 0.25 g/kg ι‐carrageenan, and 0.25 g/kg λ‐carrageenan, respectively), thereby inhibiting the formation of the casein network to different degrees. Further, our finding suggested that ι‐carrageenan and λ‐carrageenan can improve the quality of LFC; however, this has still not been confirmed.…”
Section: Introductionmentioning
confidence: 99%
“…It was still unclear that carrageenan affected cheese quality by increasing the moisture content or by interrupting the interactions between casein molecules. Our previous study (Wang and others ) showed that κ‐carrageenan, ι‐carrageenan, and λ‐carrageenan adsorb onto the surface of casein in different ways at low concentrations (for example, tail adsorption, flat adsorption, and ring adsorption for 0.2 g/kg κ‐carrageenan, 0.25 g/kg ι‐carrageenan, and 0.25 g/kg λ‐carrageenan, respectively), thereby inhibiting the formation of the casein network to different degrees. Further, our finding suggested that ι‐carrageenan and λ‐carrageenan can improve the quality of LFC; however, this has still not been confirmed.…”
Section: Introductionmentioning
confidence: 99%
“…In the presence of high concentrations of ι ‐CG and λ ‐CG, other factors may overcome the effect of additional forces, leading to the weakened gels. Our previous results showed that the recombined systems containing high concentrations of ι ‐CG and λ ‐CG carried the maximum negative charges; thus the electrostatic repulsions between the rennet‐altered casein micelles were greater than those of other recombined samples, leading to the impediment of self‐association of the particles. Therefore in ι ‐CG‐H and λ ‐CG‐H the short‐range charge repulsions may be responsible for the impaired aggregation and the following gel formation.…”
Section: Discussionmentioning
confidence: 97%
“…When a sufficient amount of κ ‐casein has been hydrolyzed, the casein micelles destabilize and begin to aggregate, which is the second stage of rennet coagulation . Our previous study indicated that carrageenan ( κ ‐CG, ι ‐CG and λ ‐CG) adsorbed onto the surface of casein micelles in different ways, consequently affecting the CMP release and aggregation behavior of pure casein micelle dispersions. However, there were still some questions that needed to be solved: (1) because the actual milk system was more complex than pure casein micelle solution, the impact of carrageenan on the rennet‐induced gelation of the skim milk system was unknown; (2) although our previous study used rheology to study the effect of carrageenan on the rennet‐induced gelation, the structural changes of casein micelles during this renneting stage were still unclear; (3) the rennet‐induced gel strength decreased with the increase in carrageenan concentration, but there was a lack of further investigations to explain this phenomenon.…”
Section: Introductionmentioning
confidence: 99%
“…At neutral pH, kappa and iota carrageenans in helical conformation can stabilize milk proteins at a low concentration since the addition of carrageenan affected the formation of rennet-induced gels, mainly attributed to electrostatic interactions between kappa casein the positive patch and negative sulfate groups of carrageenans (Snoeren et al, 1976;Thaiudom and Goff, 2003;Gu et al, 2005;Corredig et al, 2011;Wang et al, 2014). Iota, kappa and lambda carrageenans adsorb onto casein micelles forming a cross-linking network below the coil-helix transition temperature (60 °C), probably due to the bridging by the helical parts of carrageenan chains (Dalgleish and Morris, 1998;Langendorff et al, 2000;Gu et al, 2005).…”
Section: Yield Moisture Fat Phase and Proteinmentioning
confidence: 99%
“…Carrageenan conformation results in differences between adsorption behaviors due to different charge densities. Both charge density (lambda>iota>kappa) and polysaccharide conformation contribute to the structure forming event (Gu et al, 2005;Wang et al, 2014). Kappa and iota are in the helix form at ambient temperature, whereas lambda is in the random coil conformation (Nilsson and Piculell, 1991;Gu et al, 2005).…”
Section: Yield Moisture Fat Phase and Proteinmentioning
confidence: 99%