A Kinetic Study on the Heat-Induced Changes of Whey Proteins Concentrate at Two pH Values

Food and Bioprocess Technology

Volumn 5, Issue 6, 2012, Pages 2160-2171

  Stǎnciuc, Nicoleta ^a   Dumitraşcu, Loredana ^a   Ardelean, Alina ^a   Stanciu, Silvius ^a   Râpeanu, Gabriela ^a  

^a DUNAREA DE JOS UNIVERSITY OF GALATI   (Romania)

Author keywords

Functional properties; Heat treatment; Kinetic; Whey proteins

Indexed keywords

CONFORMATIONAL CHANGE; EFFECTS OF HEAT TREATMENT; FOOD INGREDIENTS; FRACTIONAL CONVERSION; FUNCTIONAL PROPERTIES; HEATING CONDITIONS; KINETIC STUDY; NUTRITIONAL QUALITIES; PH VALUE; PRODUCT CHARACTER; PROTEIN SOLUBILITY; REACTION MECHANISM; WHEY PROTEIN CONCENTRATE; WHEY PROTEINS; WHEY PROTEINS CONCENTRATE;

ARRHENIUS PLOTS; DENATURATION; HEAT TREATMENT; KINETICS; SOLUBILITY; TURBIDITY;

PROTEINS;

EID: 84864401020     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-011-0590-y     Document Type: Article

References (45)

1. Alting, A. C., Hamer, R. J., De Kruif, C. G., & Visschers, R. W. (2000). Formation of disulfide bonds in acid-induced gels of preheated whey protein isolate. Journal of Agricultural and Food Chemistry, 48, 5001-5007.
2. Alting, A. C., Weijers, M., de Hoog, E. H., van de Pijpekamp, A. M., Cohen Stuart, M. A., Hamer, R. J., et al. (2004). Acid-induced cold gelation of globular proteins: effects of protein aggregate characteristics and disulfide bonding on rheological properties. Journal of Agricultural and Food Chemistry, 52, 623-631.
3. Anema, S. G., & McKenna, A. (1996). Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. Journal of Agricultural and Food Chemistry, 44, 422-428.
4. Beveridge, T., Toma, S. J., & Nakai, S. (1974). Determination of SH and SS-groups in some food proteins using Ellman's reagent. Journal of Food Science, 39, 49-51.
5. Boye, J. I., & Alli, I. (2000). Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study. Food Research International, 33(8), 673-682.
6. Brunner, J. R. (1977). Milk Proteins. In J. R. Whitaker & S. R. Tannenbaum (Eds.), Food Proteins (pp 175-208). Wesport: AVI.
7. Cecil, R. (1963). Intramolecular bonds in proteins: The role of sulfur in proteins. In H. Neurath (Ed.), The proteins, composition, structure, and function ((pp, Vol. 1, pp. 379-476). New York: Academic.
8. Claeys, W. (2003). Intrinsic time temperature integrators for thermal and high pressure processing of milk. PhD Thesis. Katholieke Universiteit Leuven. Belgium.
9. Creighton, T. E. (1984). Proteins: Structure and molecular properties. New York: Freeman.
10. 119 is formed during heat denaturation of β-lactoglobulin. Biochemical and Biophysical Research Communications, 301, 465-471.
11. Croguennec, T., O'Kennedy, B. T., & Mehra, R. (2004). Heat-induced denaturation/aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed. International Dairy Journal, 14, 399-409.
12. Dalgleish, D. G., Senaratne, V., & François, S. (1997). Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation. Journal of Agricultural and Food Chemistry, 45, 3459-3464.
13. Dannenberg, F., & Kessler, H. G. (1988). Thermodynamic approach to kinetics of β-lactoglobulin denaturation in heated milk and sweet whey. Milchwissenschaft, 43, 139-142.
14. De la Fuente, M. A., Singh, H., & Hemar, Y. (2002). Recent advances in the characterization of heat-induced aggregates and intermediates of whey proteins. Trends in Food Science and Technology, 13, 262-274.
15. De Wit, J. N. (1990). Thermal stability and functionality of whey proteins. Journal of Dairy Science, 73, 3602-3612.
16. De Wit, J. N. (2009). Thermal behavior of bovine β-lactoglobulin at temperatures up to 1500 C. a review. Trends in Food Science and Technology, 20, 27-34.
17. De Wit, J. N., & Klarenbeek, G. (1984). Effects of various heat treatments on structure and solubility of whey proteins. Journal of Dairy Science, 67, 2701-2710.
18. De Wit, R., & Nieuwenhuijse, H. (2008). Kinetic modeling of the formation of sulfur-containing flavor components during heat-treatment of milk. International Dairy Journal, 18, 539-547.
19. Doi, E. (1993). Gels and gelling of globular proteins. Trends in Food Science and Technology, 4, 1-5.
20. Grácia-Juliá, A., René, M., Cortés-Muňoz, M., Picart, L., Lǒpez-Pedemonte, T., Chevalier, D., et al. (2008). Effect of dynamic high pressure on whey protein aggregation: A comparison with the effect of continuous short-time thermal treatments. Food Hydrocolloids, 22, 1014-1032.
21. Havea, P., Singh, H., & Creamer, L. K. (2001). Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment. The Journal of Dairy Research, 68, 483-497.
22. Hoffman MAM & van Mill PJJM. (1997). Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds. Journal of Agricultural and Food Chemistry, 45, 2942-2948.
23. Hoffman, M. A. M., Sala, G., Olieman, C., & de Kruif, K. (1997). Molecular mass distributions of heat-induced β-lactoglobulin aggregates. Journal of Agricultural and Food Chemistry, 45, 2949-2957.
24. Iametti, S., De Gregori, B., Vecchio, G., & Bonomi, F. (1996). Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. European Journal of Biochemistry, 237, 106-112.
25. Ibanoglu, E. (2005). Effect of hydrocolloids on the thermal denaturation of proteins. Food Chemistry, 90, 621-626.
26. Kato, A., Osako, Y., Matsudomi, N., & Kobayashi, K. (1983). Changes in the emulsifying and foaming properties of proteins during heat denaturation. Agricultural and Biological Chemistry, 47, 33-37.
27. Kim, D. A., Cornec, M., & Narsimhan, G. (2005). Effect of thermal treatment on interfacial properties of β-lactoglobulin. Journal of Colloid and Interface Science, 285, 100-109.
28. Law, A. J. R., & Leaver, J. (2000). Effect of pH on the thermal denaturation of whey proteins in milk. Journal of Agriculture and Food Chemistry, 48, 672-679.
29. Le Bon, C., Nicolai, T., & Durand, D. (1999). Growth and structure of aggregates of heat-denatured β-lactoglobulin. International Journal of Food Science & Technology, 34(5-6), 451-465.
30. Lyster, R. L. J. (1970). The denaturation of α-lactalbumin and β-lactoglobulin in heated milk. The Journal of Dairy Research, 37, 233-243.
31. Manderson, G. A., Hardman, M. J., & Creamer, L. K. (1999). Effect of heat treatment on bovine β-lactoglobulin A, B and C explored using thiol availability and fluorescence. Journal of Agriculture and Food Chemistry, 47, 3617-3627.
32. Meza, B. E., Verdini, R. A., & Rubiolo, A. C. (2009). Viscoelastic behavior of heat-treated whey protein concentrates suspensions. Food Hydrocolloids, 23, 661-666.
33. Morr, C. V., & Ha, E. Y. W. (1993). Whey protein concentrate and isolates: Processing and functional properties. Critical Reviews in Food Science and Nutrition, 33, 431-476.
34. Odian, G. (2004). Principles of polymerization (4th ed., pp. 408-409). Hoboken: Wiley.
35. Pantaloni, D. (1964). Étude de la transition R/S de la β-lactoglobuline par spectropolarimétrie et par spectrophotométrie de differences. Comptes Rendus Academic Science, 258, 5753-5756.
36. Sava, N., van der Plancken, I., Claeys, W., & Hendrickx, M. (2005). The kinetics of heat-induced structural changes of β-lactoglobulin. Journal of Dairy Science, 88, 1646-1653.
37. Sawyer, L. (2003). β-Lactoglobulin. In P. F. Fox & P. L. H. McSweeney (Eds.), Advanced Dairy Chemistry-1: Proteins. 3rd ed., Part A (pp. 319-386). New York: Kluwer.
38. Schmitt, C., Bovay, C., Vuilliomenet, A. M., Rouvet, M., & Bovetto, L. (2010). Influence of protein and mineral composition on the formation of whey protein heat-induced micro gels. Food Hydrocolloids. doi: 10. 1016/j. foodhyd. 2010. 05. 010.
39. Schokker, E. P., Singh, H., & Creamer, L. K. (2000). Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin. International Dairy Journal, 10, 843-853.
40. Shimada, K., & Cheftel, J. C. (1989). Sulfhydryl group/disulfide bond interchange reactions during heat induced gelation of whey protein isolate. Journal of Agriculture and Food Chemistry, 37, 161-168.
41. Simmons, M. J. H., Jayaraman, P., & Fryer, P. J. (2007). The effect of temperature and shear rate on the aggregation of whey proteins and its implications for milk fouling. Journal of Food Engineering, 79, 517-528.
42. Singh, H., & Flanagan, J. (2006). Milk proteins. In Y. H. Hui (Ed.), Handbook of Food Science, Technology, and Engineering (Vol. 1, pp. 26-31). New York: Taylor and Francis.
43. Tanford, C., Bunville, L. G., & Nozaki, Y. (1959). The reversible transformation of β-lactoglobulin at pH 7. 5. Journal of the American Chemical Society, 81, 4032-4036.
44. Walstra, P., & Jenness, R. (1984). Salts. In P. Walstra & R. Jenness (Eds.), Dairy Chemistry and Physics (pp. 42-57). New York: Wiley.
45. Ye, A., & Taylor, S. (2009). Characterization of cold-set gels produced from heated emulsions stabilized by whey protein. International Dairy Journal, 19, 721-727.