Free Access
Volume 87, Number 6, November-December 2007
Page(s) 535 - 554
Published online 04 January 2008
References of  Lait 87 (2007) 535-554
  1. Alting A.C., de Jongh H.H.J., Visschers R.W., Simons J., Physical and chemical interactions in cold gelation of food proteins, J. Agric. Food Chem. 50 (2002) 4682-4689 [CrossRef] [PubMed].
  2. Alting A.C., Hamer R.J., de Kruif C.G., Paques M., Visschers R.W., Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels, Food Hydrocoll. 17 (2003) 469-479 [CrossRef].
  3. AOAC, Official Methods of Analysis of AOAC International, Association of Official Analytical Chemists, Patricia Cunniff, Gaithersburg, USA, 1997.
  4. Barbut S., Determining water and fat holding, in: Hall G.M. (Ed.), Methods of testing prote in functionality, Chapman & Hall, London, 1996, pp. 187-225.
  5. Braga A.L.M., Menossi M., Cunha R.L., The effect of the glucono-delta-lactone/caseinate ratio on sodium caseinate gelation, Int. Dairy J. 16 (2006) 389-398 [CrossRef].
  6. Bramaud C., Aimar P., Daufin G., Thermal isoelectric precipitation of Alpha-Lactalbumin from a whey-protein concentrate - influence of protein-calcium complexation, Biotechnol. Bioeng. 47 (1995) 121-130 [CrossRef].
  7. Bramaud C., Aimar P., Daufin G., Whey protein fractionation: Isoelectric precipitation of alpha-lactalbumin under gentle heat treatment, Biotechnol. Bioeng. 56 (1997) 391-397 [CrossRef].
  8. Bryant C.M., McClements D.J., Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey, Trends Food Sci. Technol. 9 (1998) 143-151 [CrossRef].
  9. Cavallieri A.L.F., Cunha R.L., The effects of acidification rate, pH and ageing time on the acidic cold set gelation of whey proteins, Food. Hydrocoll. 22 (2007) 439-448 [CrossRef].
  10. Cheftel J.C., Cuq J.L., Lorient D., Aminoacidos, peptidos y proteinas, in: Fennema O.R. (Ed.), Química de los alimentos, Editorial Acribia, Zaragoza, 1996, pp. 275-414.
  11. Copeland R.A., Eletrophoretic and chromatographic methods for assessing protein purity, in: Copeland R.A. (Ed.), Methods for protein analysis: A practical guide to laboratory proticols, Chapman & Hall, New York, USA, 1990, pp. 59-98.
  12. Gezimati J., Singh H., Creamer L.K., Aggregation and gelation of bovine beta-lactoglobulin, alpha-lactalbumin, and serum albumin, in: Paris N., Kato A., Creamer L.K., Pearce J. (Eds.), Macromolecular Interactions in Food Technology, Amer. Chemical Soc., Washington, 1996, pp. 113-123.
  13. Havea P., Singh H., Creamer L.K., Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment, J. Dairy Res. 68 (2001) 483-497 [CrossRef] [PubMed].
  14. Havea P., Singh H., Creamer L.K., Heat-induced aggregation of whey proteins: Comparison of cheese WPC with acid WPC and relevance of mineral composition., J. Agric. Food Chem. 50 (2002) 4674-4681 [CrossRef] [PubMed].
  15. Havea P., Carr A.J., Creamer L.K., The roles of disulphide and non-covalent bonding in the functional properties of heat-induced whey protein gels, J. Dairy Res. 71 (2004) 330-339 [CrossRef] [PubMed].
  16. Hodge J.R., Hofreiter B.T., Determination of reducing sugar and carboydrates: Phenol sulfuric test, in: Whistler R.L., Wolfrom M.L. (Eds.), Methods in Carbohidrate Chemistry, Academic Press, New York, USA, 1962, pp. 380-394.
  17. Hoffmann M.A.M., van Mil P.J.J.M., Heat-induced aggregation of $\beta
$-Lactoglobulin: Role of the free thiol group and dissulphide bonds, J. Agric. Food Chem. 45 (1997) 2942-2948 [CrossRef].
  18. Hong Y.H., Creamer L.K., Changed protein structures of bovine $\beta
$-lactoglobulin B and $\alpha $-lactalbumin as a consequence of heat treatment, Int. Dairy J. 12 (2002) 345-359 [CrossRef].
  19. Ju Z.Y., Kilara A., Effects of preheating on properties of aggregates and of cold-set gels of whey protein isolate, J. Agric. Food Chem. 46 (1998) 3604-3608 [CrossRef].
  20. Laemmli U.K., Cleavage of structural proteins during assembly of head of bacteriophage-T4, Nature 227 (1970) 680-685 [CrossRef] [PubMed].
  21. Livney Y.D., Corredig M., Dalgleish D.G., Influence of thermal processing on the properties of dairy colloids, Curr. Opin. Colloid Interface Sci. 8 (2003) 359-364 [CrossRef].
  22. Lupano C.E., Effect of heat-treatments in very acidic conditions on whey-protein isolate properties, J. Dairy Sci. 77 (1994) 2191-2198.
  23. Lupano C.E., Gelation of mixed systems whey protein concentrate-gluten in acidic conditions, Food Res. Int. 33 (2000) 691-696 [CrossRef].
  24. Lupano C.E., Dumay E., Cheftel J.C., Gelling properties of whey-protein isolate - influence of calcium removal by dialysis or diafiltration at acid or neutral pH, Int. J. Food Sci. Technol. 27 (1992) 615-628.
  25. Lupano C.E., Renzi L.A., Romera V., Gelation of whey protein concentrate in acidic conditions: Effect of pH, J. Agric. Food Chem. 44 (1996) 3010-3014 [CrossRef].
  26. Morr C.V., Ha E.Y.W., Whey protein concentrates and isolates: Processing and functional properties, Crit. Rev. Food Sci. Nutr. 33 (1993) 431-476 [PubMed].
  27. Puppo M.C., Lupano C.E., Anon M.C., Gelation of soybean protein isolates in acidic conditions - effect of pH and protein-concentration, J. Agric. Food Chem. 43 (1995) 2356-2361 [CrossRef].
  28. Schokker E.P., Singh H., Creamer L.K., Heat-induced aggregation of $\beta
$-lactoglobulin A and B with $\alpha $-lactalbumin, Int. Dairy J. 10 (2000) 843-853 [CrossRef].
  29. Shimada K., Cheftel J.C., Texture characteristics, protein solubility, and sulfhydryl-group disulfide bond contents of heat-induced gels of whey-protein isolate, J. Agric. Food Chem. 36 (1988) 1018-1025 [CrossRef].
  30. Steffe J.F., Rheological methods in food process engineering, Freeman Press, East Lansing, USA, 1996.
  31. Vardhanabhuti B., Foegeding A., Rheological properies and characterization of polymerized whey protein isolates, J. Agric. Food Chem. 47 (1999) 3649-3655 [CrossRef] [PubMed].
  32. Vojdani J., Solubility, in: Hall G.M. (Ed.), Methods of testing protein functionality, Chapman & Hall, London, UK, 1996, pp. 11-55.