[en] Since proteose-peptone is a mixture of heterogeneous proteins and peptides, its functional properties have not yet been fully understood. The present study was undertaken to elucidate the emulsifying properties of proteose-peptones and a parallel evaluation was performed of the emulsifying activity of the total fraction prepared from bulk skimmed milk by precipitation with ammonium sulphate and of the most hydrophobic fraction purified by hydrophobic interaction fast protein liquid chromatography. A turbidimetric technique was used and the absorbance value at 500 nm was then directly used as the emulsifying activity index. The results obtained confirmed the good emulsifying activity of this protein fraction of the whey and demonstrated the considerable influence of the concentration on the capacity of the proteose-peptones to stabilize a model oil-in-water emulsion. Moreover, at all the concentrations examined, the purified component 3 showed a higher emulsifying activity than the total unpurified fraction. (C) 1999 Elsevier Science Ltd. All rights reserved.
Britten, M. and Giroux, H. J. (1993) Interfacial properties of milk protein-stabilized emulsions as influenced by protein concentration. Journal of Agricultural and Food Chemistry 41, 1187-1191.
Courthaudon, D., Girardet, J. M., Chapal, C., Lorient, D. and Linden, G. (1985) Surface activity and competitive adsorption of milk component 3 and porcine pancreatic lipase at the dodecane-water interface. In Foods Macromolecules and Colloids, eds E. Dicknison and D. Lorient. Royal Society of Chemistry, Cambridge, pp 58-69.
Elizalde, B. E., De Kanterewicz, R. J., Pilosof, A. M. R. and Bartholomai, G. B. (1988) Physicochemical properties of food proteins related to their ability to stabilize oil-in-water emulsions. Journal of Food Science 53, 845-848.
Girardet, J. M., Mati, A., Sanogo, T., Etienne, L. and Linden G. (1991) Fast protein liquid chromatography purification of hydrophobic fraction of bovine milk proteose-peptone and characterization by bidimensional electrophoresis. Journal of Dairy Research 58, 85-98.
Girardet, J. M., Linden, G., Loye, S., Courthaudon, J. L., Lorient, D. (1993) Study of mechanism of lipolysis inhibition by bovine milk proteose-peptone component 3. Journal of Dairy Science 76, 2156-2161.
Girardet, J. M. and Linden, G. (1996) PP3 component of bovine milk: a phosphorylated whey glycoprotein. Journal of Dairy Research 63, 333-350.
Halling, P. J. (1981) Protein-stabilized foams and emulsions. CRC Critical Review in Food Science and Nutrition 13, 155-170.
Haque, Z. and Kinsella, J. E. (1989) Emulsifying properties of food proteins: development of a standardized emulsification method. Journal of Food Science 54, 39-44.
Innocente, N., Corradini, C., Blecker, C. and Paquot, M. (1998) Dynamic surface properties of the proteose-peptone fraction of bovine milk. Journal of Dairy Science 81, 1833-1839.
Leman, J., Haque, Z. and Kinsella, J. E. (1988) Creaming stability of fluid emulsions containing different milk protein preparations. Milchwissenschaft 43, 286-289.
Nejjar, J., Paquet, D. and Linden, G. (1990) The PP3 component of the proteose-peptone. Extraction from unheated skim milk. Milchwissenscaft 45, 84-87.
Paquet, D., Nejjar, J. and Linden, G. (1988) Study of a hydrophobic protein fraction isolated from milk proteose-peptone. Journal of Dairy Research 71, 1464-1469.
Pâquet, D. (1989) Revue bibliographique: la fraction protéose-peptones du lait. Le lait 69, 1-21.
Pearce, K. N. and Kinsella, J. E. (1978) Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 26, 716-723.
Shimizu, M., Yamauchi, K. and Saito, M. (1989) Emulsifying properties of the proteose-peptone fraction obtained from bovine milk. Milchwissenschaft 44, 497-500.
Sorensen, E. S. and Petersen, E. T. (1993) Purification and characterization of three proteins isolated from the proteose-peptone fraction of bovine milk. Journal of Dairy Research 60, 189-192.
Tornberg, E. (1977) Review: the application of the drop volume technique to measurements of the adsorption of proteins at interfaces. Journal Colloid and Interface Science 3, 391-400.
