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Gelation of whey proteins

Bolder, S.G., Hendrickx, H., Sagis, L.M.C., van der Linden, E. (2006). Ca2+-induced cold-set gelation of whey protein isolate fibrils. Applied Rheology, 16, 258- 264. [Pg.26]

The gelation of whey protein has also been shown to be affected by the presence of lipids and the presence of lactose (29). [Pg.138]

Aguilera, J.M. 1995. Gelation of whey proteins. Food Technol. 49(10), 83-89. [Pg.60]

The formation of beads is a two-step process based on the cold gelation of whey proteins in the presence of divalent cations, such as Ca2+ [67], Briefly, the whey protein isolate (WPI) solution (10% w/v in deionized water) was (i) adjusted at pH 7 to favor the apparition of negative charges implied in ionic bounds with Ca2+ ions and (ii) heated (80 °C, 45 min) to denaturate the proteins. Recombinant cells in the beginning of their stationnary growth phase were suspended in a sterile solution of... [Pg.580]

Hongsprabhas, P., and Barbut, S. (1998), Ca2+-induced cold gelation of whey protein isolate Effect of two-stage gelation, Food Res. Int., 30, 523-527. [Pg.589]

Monteiro, S. R., Tavares, C. A., Evtuguin, D. V, Moreno, N., and Lopes da Silva, J. A. 2005. Influence of galactomannans with different molecular weights on the gelation of whey proteins at neutral pH. [Pg.397]

Boye, ], Alii, ], Ramaswamy, H, and Raghavan, V, (1997), Interactive effects of factors affecting gelation of whey proteins. /. Food Sci. 62, 57-65,... [Pg.483]

Britten, M., and Giroux, H.J. (2001). Acid-induced gelation of whey protein polymers Effects... [Pg.30]

Eissa, A.S., Bisram, S., and Khan, S.A. (2004). Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme. J. Agric. Food Chem. 52, 4456- 464. Euston, S.R., Finnigan, S.R., and Hirst, R.L. (2001). Heat-induced destabilization of oil-in-... [Pg.32]

Ju, Z.Y., Otte, J., Zakora, M., and Qvist, K.B. (1997). Enzyme-induced gelation of whey proteins Effect of protein denaturation. Int. Dairy J. 7, 71-78. [Pg.33]

Mangino, M.E. (1992). Gelation of whey protein concentrates. Food Technol. 46(1), 114, 116-117. [Pg.34]

Hongsprabhas, R and Barbut, S. 1997. Protein and salt effects on Ca -induced gelation of whey protein isolate. Journal of Food Science 62 382-385. [Pg.279]

Sadeghi S, Madadlou A, Yarmand M. Microemulsification-cold gelation of whey proteins for nanoencapsulation of date pahn pit extract. Food Hydrocolloids 2014 35 590-596. [Pg.761]

Beaulieu, L., Savoie, L., Paquin, P., Subirade, M. (2002). Elaboration and characterization of whey protein beads by an emulsification/cold gelation process application for the protection of retinol. Biomacromolecules, 3, 239-248. [Pg.70]

Although the gelation properties of whey proteins are of great importance in many foods (Mulvihill, 1992) and it is possible to form a weak gel in creams by the formation of a continuous network of fat globules, most important milk gels are those involving casein micelles which can be made to form a gel matrix either by isoelectric precipitation (acid-induced gel) or by the action of a proteolytic enzyme (rennet-induced gel). Both gel types... [Pg.374]

Enzymatic gelation of partially heat-denatured whey proteins by trypsin, papain, pronase, pepsin, and a preparation of Streptomyces griseus has been studied (Sato et al., 1995). Only peptic hydrolysate did not form a gel. The strength of the gel depended on the enzyme used and increased with increasing DH. Hydrolysis of whey protein concentrate with a glutamic acid specific protease from Bacillus licheniformis at pH 8 and 8% protein concentration has been shown to produce plastein aggregates (Budtz and Nielsen, 1992). The viscosity of the solution increased dramatically during hydrolysis and reached a maximum at 6% DH. Incubation of sodium caseinate with pepsin or papain resulted in a 55-77% reduction in the apparent viscosity (Hooker et al., 1982). [Pg.40]

Tziboula, A. and Home, D. S. 1999. Influence of whey protein denaturation on re-carrageenan gelation. Colloid Surf. B Biointeifaces 12 299-308. [Pg.400]

As with other viscous polyanions such as carrageenan, pectin may be protective towards milk casein colloids, enhancing the properties (foam stability, solubility, gelation and emulsification) of whey proteins whilst utilizing them as a source of calcium. [Pg.65]

Schorsch et al. (2001) examined the effects of denaturation of whey proteins in the presence and absence of casein micelles on gel properties. Heat treatment sequence was found to influence the acid gelation properties of casein-whey mixtures. Denaturation of whey proteins in the absence of casein micelles induced more rapid gelation on addition of acid. Gels made from these milks had a more particulate gel structure than gels made from casein-whey mixtures which were heated without prior denaturation of the whey proteins. [Pg.12]

Blends of whey protein isolate and denatured whey protein isolates were microparticulated using a microfluidizer prior to the formation of heat-set gels. Increasing the number of passes in the microfluidizer increased the hardness of the gels, an effect attributed in part to the more homogenous gelation of smaller aggregates (Sanchez et al., 1999). [Pg.16]


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See also in sourсe #XX -- [ Pg.153 ]




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