Phosphorylation of β-lactoglobulin using amino acids as the sole base and nucleophile of the reaction

Journal of Protein Chemistry - Tập 14 Số 3 - Trang 145-150 - 1995
Mahmoud Sitohy1, Jean‐Marc Chobert1, Tomasz Haertlé1
1Laboratoire d'Etude des Interactions des Molécules Alimentaires, Institut National de la Recherche Agronomique, B.P. 627, 44316, Nantes Cedex 03, France

Tóm tắt

Từ khóa


Tài liệu tham khảo

Bartlett, G. R. (1959). Phosphorus assay in column chromatography,J. Biol. Chem. 234, 466–468.

Bidlingmeyer, B. A., Cohen, S. A., and Tarvin, T. L. (1984). Rapid analysis of amino acids using pre-column derivatization,J. Chromatogr. 336, 93–104.

Chobert, J.-M, Touati, A., Bertrand-Harb, C., Dalgalarrondo, M., and Nicolas, M.-G. (1989). Solubility and emulsifying properties of kappa casein and its caseinomacropeptide,J. Food Biochem. 13, 457–473.

Chobert, J.-M., Touati, A., Bertrand-Harb, C., Dalgalarrondo, M., Nicolas, M.-G., and Haertlé, T. (1991).In vitro proteolysis and functional properties of reductively alkylatedβ-casein derivatives,J. Dairy Res. 58, 285–298.

Dagorn-Scaviner, C., Guēguen, J., and Lefebvre, J. (1987). Emulsifying properties of pea globulins as related to their adsorption behaviours,J. Food Sci. 52, 335–341.

Guillerme, C., Loisel, W., Bertrand, D., and Popineau, Y. (1993). Study of foam stability by video image analysis: relationship with the quantity of liquid in the foam,J. Texture Studies 24, 287–302.

Hirotsuka, M., Taniguchi, H., Narita, H., and Kito, M. (1984). Functionality and digestibility of a highly phosphorylated soybean protein,Agric. Biol. Chem. 48, 93–100.

Huang, Y.-T., and Kinsella, J. E. (1987). Effect of phosphorylation on emulsifying and foaming properties and digestibility of yeast protein,J. Food Sci. 52, 1684–1688.

Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of the bacteriophage T4,Nature 227, 680–685.

Lehninger, A. L. (1981). InBiochemistry, the Molecular Basis of Cell Structure and Function, Flammarion médecine sciences, p. 76.

Loisel, W., and Popineau, Y. (1993). Procédé et matériel de caracterisation de la stabilité d'une émulsion, Demande de brevet francais.

Loisel, W., Gueguen, J., and Popineau, Y. (1993). A new apparatus for analysing foaming properties of proteins,Food Proteins: Structure and Functionality (Schwenke, K. D., and Mothes, R., eds.), VCH, Weinheim, pp. 320–323.

Mailliart, P., and Ribadeau Dumas, B. (1988). Preparation ofβ-lactoglobulin andβ-lactoglobulin free proteins from whey retentate by NaCl salting out at lowpH,J. Food Sci. 53, 343–347.

Matheis, G., Penner, H. M., Feeney, R. E., and Whitaker, J. R. (1983). Phosphorylation of casein and lysozyme by phosphorus oxychloride,J. Agric. Food Chem. 31, 379–387.

Medina, A. L., Colas, B., Le Meste, M., Renaudet, I., and Lorient, D. (1992). Physicochemical and dynamic properties of caseins modified by chemical phosphorylation,J. Food Sci. 57, 617–620.

Sitohy, M., Chobert, J.-M., and Haertlé, T. (1994a). Influence of the reaction conditions on the chemical phosphorylation of milk proteins,Milchwissenschaft, in press.

Sitohy, M., Chobert, J.-M., and Haertlé, T. (1994b). Phosphorylation of β-lactoglobulin under mild conditions,J. Agric. Food Chem., to appear.

Sung, H.-Y., Chen, H.-J., Liu, T., and Su, J.-C. (1983). Improvement of functionality of soy protein isolate through chemical phosphorylation,J. Food Sci. 48, 716–721.

Woo, S. L., Creamer, L. K., and Richardson, T. (1982). Chemical phosphorylation of bovineβ-lactoglobulin,J. Agric. Food Chem. 30, 65–69.