Adsorption of β-lactoglobulin variants A and B to the air-water interface

International Journal of Food Science and Technology

Volumn 34, Issue 5-6, 1999, Pages 509-516

  Mackie, Alan R ^a   Husband, Fiona A ^a   Holt, Carl ^b   Wilde, Peter J ^a  

^a INSTITUTE OF FOOD RESEARCH   (United Kingdom)

^b HANNAH RESEARCH INSTITUTE   (United Kingdom)

Author keywords

Adsorption; Air water interface; Surface rheology; Surface tension; lactoglobulin

Indexed keywords

EID: 0000810176     PISSN: 09505423     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2621.1999.00315.x     Document Type: Article

References (32)

1. Armstrong, J.M., McKenzie, H.A. & Sawyer, W.H. (1967). On the fractionation of β-lactoglobulin and α-lactalbumin. Biochimica Biophysica Acta, 147, 60-72.
2. Clark, D.C., Wilde, P.J., Wilson, D.R. & Wüstneck, R. (1992). The interaction of sucrose esters with β-lactoglobulin and β-casein from bovine milk. Food Hydrocolloids, 6, 173-186.
3. Closs, B., Courthaudon, J.L. & Lorient, D. (1990). Effect of glycosylation on the surface properties of the soluble fraction of casein. Journal of Food Science, 55, 437-439.
4. Coke, M., Wilde, P.J., Russell, E.J. & Clark, D.C. (1990). The influence of surface composition and molecular diffusion on the stability of foams formed from protein detergent mixtures. Journal of Colloid and Interface Science, 138, 489-504.
5. Cornec, M., Wilde, P.J., Gunning, P.A., Mackie, A.R., Husband, F.A., Parker, M.L. & Clark, D.C. (1998). Emulsion stability as affected by competitive adsorption between an oil-soluble emulsifier and milk proteins at the interface. Journal of Food Science, 63, 39-43.
6. Damon, A.J.H. & Kresheck, G.C. (1982). Influence of surfactants on the conformation of β-lactoglobulin B using circular dichroism. Biopolymers, 21, 895-908.
7. Das, K.P. & Kinsella, J.E. (1989). pH dependent emulsifying properties of β-lactoglobulin. Journal of Dispersion Science and Technology, 10, 77-102.
8. Elofsson, U.M., Paulsson, M.A. & Arnebrant, T. (1997a). Adsorption of β-lactoglobulin A and B in relation to self association: effect of concentration and pH. Langmuir, 13, 1695-1700.
9. Elofsson, U.M., Paulsson, M.A. & Arnebrant, T. (1997b). Adsorption of β-lactoblobulin A and B: effect of ionic strength and phosphate ions. Colloids and Surfaces B: Biointerfaces, 8, 163-169.
10. Elofsson, U.M., Paulsson, M.A., Sellers, P. & Arnebrant, T. (1996). Adsorption during heat treatment related to the thermal unfolding/aggregation of β-lactoglobulins A and B. Journal of Colloid and Interface Science, 183, 408-415.
11. Euston, S.R., Hirst, R.L. & Hill, J.P. (1999). The emulsifying properties of β-lactoglobulin genetic variants A, B and C. Colloids and Surfaces B: Biointerfaces, 12, 193-202.
12. Foegeding, E.A., Kuhn, P.R. & Hardin, C.C. (1992). Specific divalent cation induced changes during gelation of β-lactoglobulin. Journal of Agricultural and Food Chemistry, 40, 2092-2097
13. Green, R.J., Hopkinson, I. & Jones, R.A.L. (1999). Conformational changes of globular proteins in solution and adsorbed at interfaces investigated by FT1R spectroscopy. In: Food Emulsions and Foams Interfaces, Interactions and Stability (edited by E. Dickinson & J. M. Rodriguez Patino), pp. 285-295 London: Royal Society of Chemistry (Special publication no. 227).
14. Hoffmann, M.A.M., Roefs, S.P.F.M., Verheul, M., Van Mil, J.J. M. & De Kruif, C.G. (1996). Aggregation of β-lacloglobulin studied by in situ light scattering. Journal of Dairy Research, 63, 423-440.
15. Holt, C., Waninge, R., Sellers, P., et al. (1998). Comparison of the effect of heating on the thermal denaturation of 9 different β-lactoglobulin presss of genetic variants A, B or A/B, as measured by microcalorimetry. International Dairy Journal, 8, 99-104.
16. Horiuchi, T., Fukishima, D., Sugimoto, H. & Hattori, T. (1978). Studies on enzyme-modified proteins as foaming agents: effect of structure on foam stability. Food Chemistry, 3, 35-42.
17. Huang, X.L., Catignani, G.L. & Swaisgood, H.E. (1994). Relative structural stabilities of β-lactoglobulins A and B as determined by proteolytic susceptibility and differential scanning calorimetry. Journal of Agricultural and Food Chemistry, 42, 1276-1280.
18. Jones, M.N. & Wilkinson, A. (1976). The interaction between β-lactoglobulin and sodium-n-dodecyl sulfate. Biochemical Journal, 153, 713-718.
19. Kokelaar, J.J., Prins, A. & De Gee, M. (1991). A new method for measuring the surface dilational modulus of a liquid. Journal of Colloid and Interface Science, 146, 507-511.
20. Luey, J-K., McGuire, J. & Sproull, R.D. (1991). The effect of pH and NaCI on the adsorption of β-lactoglobulin at hydrophilic and Hydrophobic silicon surfaces. Journal of Colloid and Interface Science, 143, 489-500.
21. Mackie, A.R., Gunning, A.P., Wilde, P.J. & Morris, V.J. (1999). Orogenic displacement of protein from the air/water interface by competitive adsorption. Journal of Colloid and Interface Science, 210, 157-166.
22. Manderson, G.A., Hardman, M.J. & Creamer, L.K. (1998). Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C. Journal of Agricultural and Food Chemistry, 46, 5052-5061.
23. Mitchell, J.R. (1986). Foaming and emulsifying properties of proteins. In: Developments in Food Proteins - 4 (edited by B.J.F. Hudson). Pp. 291-338. London: Elsevier.
24. Papiz, M.Z., Sawyer, L., Eliopoulos, E.E., North, A.C.T., Findlay, J.B.C., Sivaprasadarao, R., Jones, T.A., Newcomer, M.E. & Kraulis, P.J. (1986). The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature. 324, 383-385.
25. Qi, X.L., Brownlow, S., Holt, C. & Sellers, P. (1995). Effect of concentration on the denaturation of β-lactoglobulin near neutral pH. Biochimica et Biophysica Acta, 1248, 43-49.
26. Renard, D., Lefebvre, J., Griffin, M.C.A. & Griffin, W.G. (1998). Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies. International Journal of Biological Macromolecules, 22, 41-49.
27. Shimizu, M., Saito, M. & Yamauchi, K. (1985). Emulsifying and structural properties of β-lactoglobulin at different pH's. Agricultural and Biological Chemistry, 49, 189-194.
28. Timasheff, S.N., Mescanti, L., Basen, J.J. & Townend, R. (1966). Conformational transitions of bovine β-lactoglobulins A, B and C. Journal of Biological Chemistry, 241, 2496-2501.
29. Wahlgren, M. & Elofsson, U. (1997). Simple models for adsorption kinetics and their correlation to the adsorption of β-lactoglobulin A and B. Journal of Colloid and Interface Science, 188, 121-129.
30. Waniska, R.D. & Kinsella, J.E. (1985). Surface properties of β-lactoglobulin: adsorption and rearrangement during film formation. Journal of Agricultural and Food Research, 33, 1143-1148.
31. Wilde, P.J. & Clark, D.C. (1993). The competitive displacement of β-lactoglobulin by Tween-20 from oil-water and air water interfaces. Journal of Colloid and Interface Science, 155, 48-54.
32. Wong, D.W.S., Camirand, W.M. & Pavlath, A.E. (1996). Structures and functionalities of milk proteins. Critical Reviews in Food Science and Nutrition, 36, 807-844.