Foaming properties of sweet whey solutions as modified by thermal treatment

Food Chemistry

Volumn 100, Issue 2, 2007, Pages 794-799

  Tosi, E ^a   Canna, L ^a   Lucero, H ^a   Re E ^a  

^a UNIVERSIDAD TECNOLÓGICA NACIONAL   (Argentina)

Author keywords

Cheese sweet whey; Foam; Foam stabilization; Foaming agent

Indexed keywords

FOAMING AGENT;

ARTICLE; FOAM STABILITY; FOAMING; HEAT TREATMENT; SAMPLE; SWEETNESS; WHEY;

EID: 33745242338     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2005.11.001     Document Type: Article

References (41)

1. AOAC, (Association of Official Analytical Chemists) (1995). Method 930.29 and 930.30 (16th ed.). AOAC, Gaithersburg, MD, USA: AOAC.
2. Aymard D., Durand D., and Nicolai T. A comparison of the structure of β-lactoglobulin aggregates formed at pH 7 and pH 2. International Journal of Polymer Analysis and Characterization 2 (1996) 115-119
3. Aymard D., Nicolai T., Durand D., and Clark A. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules 32 (1999) 2542-2552
4. Andrews A.T. The composition, structure and origin of protease peptone component of bovine milk. European Journal of Biochemistry 90 (1978) 59-65
5. Andrews A.T. The formation and structure of protease peptone components. Journal of Dairy Research 46 (1979) 215-218
6. Atkinson P., Dickinson D., Horne D., and Richardson R. A neutron reflectivity study of the adsorption of β-lactoglobulin at the air-water interface. In: Dickinson E., and Lorient D. (Eds). Food macromolecules and colloids (1995), Royal Society of Chemistry, Cambridge 77-80
7. Bals A., and Kulozik U. Effect of pre-heating on the foaming properties of whey protein isolate using a membrane foaming apparatus. International Dairy Journal 13 (2003) 903-908
8. Banavara D.S., Anupama D., and Rankin S.A. Studies on physicochemical and functional properties of commercial sweet whey powders. Journal of Dairy Science 86 (2003) 3866-3875
9. Bauer R., Carrota R., Rischel C., and Øgendal L. Characterization and isolation on intermediate in β-lactoglobulin heat aggregation at high pH. Biophysical Journal 79 (2000) 1030-1038
10. Closs, B. (1990). Influence des traitement thermique. Influence de la Structure sur les Propiétés de Surface des Protéines du Lactosérum. (pp. 161-172). These Doctoral de l'Université de Bourgogne. Dijon, Cote-D' Or, Bourgogne, France.
11. Dalgleish D., Senaratne V., and François S. Interactions between α-lactoalbumin and β-lactoglobulin in the early stages of heat denaturation. Journal of Agricultural Food Chemistry 45 (1997) 3459-3464
12. Damodaran S. Protein stabilized foams and emulsions. In: Damodaran S., and Paraf A. (Eds). Food proteins and their applications (1997), Marcel Dekker Inc, New York 77-94
13. Dumay E., and Cheftel C. Chauffage d'un concentré protéique de β-lactoglobulin en milieu faiblement alcalin. Effet sur la solubilité et le comportement chromatographique de β-lactoglobulin et de l' α-lactoalbumin. Sciences des Aliments 9 (1989) 561-565
14. Elfagm A., and Wheelock J. Heat interaction between α-lactalbumin, β-lactoglobulin and casein in bovine milk. Journal of Dairy Science 61 (1978) 159-163
15. Gennes P. Polymers at an interface: a simplified view. Advances in Colloid and Interface Science 27 (1987) 189-193
16. Gimel J., Durand D., and Nicolai T. Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins. Macromolecules 27 (1994) 583-589
17. Guillerme C., Loisel W., Bertrand D., and Popineau Y. Study of foam stability by video images analysis: relationship with the quantity of the liquid on the foams. Journal of Texture Studies 24 (1993) 287-302
18. Havea P., Singh H., and Creamer L. Formation a new protein structures in heated mixture of BSA and α lactoalbumin. Journal of Agricultural Food Chemistry 48 (2000) 1548-1556
19. Havea P., Singh H., and Creamer L. Characterization of heat-induced aggregates of β lactoglobulin, α lactoalbumin and bovine serum albumin in a whey protein concentrate environment. Journal of Dairy Research 68 (2001) 483-497
20. Hines M., and Foegeding E. Interactions of α-lactoalbumin and bovine serum albumin with β-lactoglobulin in thermally induced gelation. Journal of Agricultural Food Chemistry 41 (1993) 341-346
21. Hoffmann M., Roefs M., Verheul M., van Mil M., and of Kruif G. Aggregation of β-lactoglobulin studied by in situ light scattering. Journal of Dairy Research 63 (1996) 423-440
22. Iametti S., Cairoli S., De Gregori B., and Bonomi F. Modifications of high-order upon heating of β lactoglobulin: dependence on the protein concentration. Journal of Agricultural Food Chemistry 43 (1995) 53-58
23. a:1974. Bruxelles, Belgique.
24. Kinsella J. Milk proteins: physicochemical and functional properties. CRC Critical reviews in food science and nutrition 21 (1984) 197-200
25. Kitabatake N., Wada R., and Fujita Y. Reversible conformational change in β-lactoglobulin A modified with N-ethylmaleimide and resistance to molecular aggregation on heating. Journal of Agricultural Food Chemistry 49 (2001) 4011-4018
26. Le Bon C., Nicolai T., and Durand D. Growth and structures of aggregates of heat-denatured β-lactoglobulin. International Journal of Food Science and Technology 34 (1999) 451-466
27. Le Meste M., Colas B., Simatos D., Closs B., Courthaudon J., and Lorient D. Contribution of protein flexibility to the foaming properties of casein. Journal of Food Science 55 (1990) 1445-1449
28. Loisel, W., Guéguen, J., & Popineau, T. (1993). A new apparatus for analyzing foaming properties of proteins. In K. D. Schwenke, & R. Mothes (Eds.), Food proteins: Structure and funcionality (pp. 320-323), New York.
29. Lorient D., Closs B., and Courthaudon J. Connaissance nouvelles sur les propiétés fonctionnelles des proteinés du lait et des dérivés. Le Lait 71 (1991) 141-171
30. Matsumura Y., Mitsui S., Dickinson E., and Mori T. Competitive adsorption of α-lactoalbumin in the molten globule state. Food Hydrocolloids 8 (1994) 555-566
31. Parris N., Purcell M., and Ptaskhin S. Thermal denaturation of whey proteins in skim milk. Journal of Agricultural Food Chemistry 39 (1991) 2167-2172
32. Pessen H., Purcell J., and Farrel Jr. H. Proton relaxation rates of water in dilute solutions of β-lactoglobulins. Determination of cross relaxation and correlations with structural changes by use of two genetic variants of self-associating globular protein. Biochimica et Biophysica Acta 828 (1985) 1-12
33. Phillips L., Hawks S., and Kinsella J. pH and heat treatment effects on foaming of whey protein isolate. Journal of Food Science 55 (1990) 1116-1120
34. Pilosof, A. M., & Bartholomai, G. (2000). Propiedades superficiales. In A. M. Pilosof & G. Bartholomai (Eds.), Caracterización Funcional y estructural de Proteinas (pp. 65-70). Eudeba.
35. Photchanachai S., and Kitabatake N. Heating of β-lactoglobulin A solution in a closed system at high temperature. Journal of Food Science 66 (2001) 647-652
36. Prabakaran S., and Damodaran S. Thermal unfolding of β lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. Journal of Agricultural Food Chemistry 45 (1997) 4303-4308
37. Robin O., Turgeon S., and Paquin P. Functional properties of milk proteins. In: Hui Y.H. (Ed). Dairy science and technology handbook. 1. Principles and properties (1993), VCH Publisher, New York 227-231
38. Roefs M., and of Kruif K. A model for denaturation and aggregation of β lactoglobulin. European Journal of Biochemistry 226 (1994) 883-889
39. Shimada K., and Cheftel C. Sulfhydryl group disulfide bond interchange reactions during eat-induced gelation of whey protein isolate. Journal of Agricultural Food Chemistry 37 (1989) 161-168
40. Schokker E., Singh H., Pinder D., and Creamer L. Heat-induced aggregation of β lactoglobulin A and B with α lactoalbumin. International Dairy Journal 10 (2000) 843-853
41. Townsend A., and Nakai S. Relationship between hydrophobicity and foaming characteristics of food proteins. Journal of Food Science 48 (1983) 588-589