The adsorption-induced secondary structure of β-casein and of distinct parts of its sequence in relation to foam and emulsion properties

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1430, Issue 1, 1999, Pages 73-83

  Caessens, Petra W J R ^a   De Jongh, Harmen H J ^a   Norde, Willem ^b   Gruppen, Harry ^b  

^a TNO   (Netherlands)

^b WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Casein; Circular dichroism; Peptide; Protein structure; Structure function relationship; Teflon interface

Indexed keywords

BETA CASEIN;

ADSORPTION; ARTICLE; CIRCULAR DICHROISM; EMULSION; FOAM; IN VITRO STUDY; IONIC STRENGTH; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; SURFACE PROPERTY;

CASEINS; CIRCULAR DICHROISM; EMULSIONS; HYDROGEN-ION CONCENTRATION; OSMOLAR CONCENTRATION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

EID: 0033028963     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00274-X     Document Type: Article

References (38)

1. H.E. Swaisgood, Chemistry of milk protein, in: P.F. Fox (Ed.), Developments in Dairy Chemistry, Part I, Proteins, Applied Science Publishers, London, 1982, pp. 1-60.
2. P. Walstra, R. Jenness, Dairy Chemistry and Physics, Wiley-Interscience, New York, 1984, 467 pp.
3. L.G. Phillips, D.M. Whitehead, J. Kinsella, Structure-Function Properties of Food Proteins, Academic Press, London, 1994, 271 pp.
4. Wong D.W.S., Camirand W.M., Pavlath A.E. Structures and functionalities of milk proteins. Crit. Rev. Food Sci. Nutr. 36:1996;807-844.
5. Dickinson E. Protein-stabilized emulsions. J. Food Eng. 22:1994;59-74.
6. Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
7. s1- and β-casein in solution. Arch. Biochem. Biophys. 211:1981;689-696.
8. 1. Int. J. Biol. Macromol. 6:1984;155-161.
9. Horne D.S. Protein-stabilized emulsions. Curr. Opin. Colloid Interface Sci. 1:1996;752-758.
10. Caessens P.W.J.R., Gruppen H., Visser S., van Aken G.A., Voragen A.G.J. Plasmin hydrolysis of β-casein: foaming and emulsifying properties of the fractionated hydrolysate. J. Agric. Food Chem. 45:1997;2935-2941.
11. P.W.J.R. Caessens, H. Gruppen, Ch.J. Slangen, S. Visser, A.G.J. Voragen, Functionality of β-casein peptides: importance of amphipathicity for emulsion stabilizing properties, (1998) submitted.
12. Dalgleish D.G. The conformation of proteins on solid/water interfaces. Caseins and phosvitin on polystyrene latices. Colloids Surf. 46:1990;141-155.
13. Dalgleish D.G., Leaver J. The possible conformations of milk proteins adsorbed on oil/water interfaces. J. Colloid Interface Sci. 141:1991;288-294.
14. Norde W., Favier J.P. Structure of adsorbed and desorbed proteins. Colloids Surf. 64:1992;87-93.
15. Smith L.J., Clark D.C. Measurement of the secondary structure of adsorbed protein by circular dichroism. 1. Measurement of the helix content of adsorbed melittin. Biochim. Biophys. Acta. 1121:1992;111-118.
16. Kondo A., Urabe T. Temperature dependence of activity and conformational changes in α-amylases with different thermostability upon adsorption on ultrafine silica particles. J. Colloid Interface Sci. 174:1995;191-198.
17. Maste M.C.L., Pap E.H.W., van Hoek A., Norde W., Visser A.J.W.G. Spectroscopic investigation of the structure of a protein adsorbed on a hydrophobic latex. J. Colloid Interface Sci. 180:1996;632-633.
18. Maste M.C.L., Norde W., Visser A.J.W.G. Adsorption-induced conformational changes in the serine proteinase Savinase: a tryptophan-fluorescence and circular dichroism study. J. Colloid Interface Sci. 196:1997;224-230.
19. Zoungrana T., Findenegg G.H., Norde W. Structure, stability, and activity of adsorbed enzymes. J. Colloid Interface Sci. 190:1997;437-448.
20. Fang Y., Dalgleish D.G. Conformation of β-lactoglobulin studied by FTIR: effect of pH, temperature, and adsorption to the oil-water interface. J. Colloid Interface Sci. 196:1997;292-298.
21. Enser M., Bloomberg G.B., Brock C., Clark D.C. De novo design and structure-activity relationships of peptide emulsifiers and foaming agents. Int. J. Biol. Macromol. 12:1990;118-124.
22. Carey K.B., Kelly S.M., Price N.C., O'Sullivan D.J., Sheehan D. Two amphiphilic, synthetic peptides display strong emulsification properties. Food Chem. 50:1994;83-85.
23. Saito M., Ogasawara M., Chikuni K., Shimizu M. Synthesis of a peptide emulsifier with an amphiphilic structure. Biosci. Biotechnol. Biochem. 3:1995;388-392.
24. Kang J.H., Lee M.K., Kim K.L., Hahm K.-S. The relationships between biophysical activity and the secondary structure of synthetic peptides from the pulmonary surfactant protein SP-B. Biochem. Mol. Biol. Int. 40:1996;617-627.
25. D. Sheehan, K. Carey, S. O'Sullivan, Design of emulsification peptides, in: S.L. Taylor (Ed.), Advances in Food and Nutrition Research, vol. 42, Academic Press, London, 1998, pp. 93-129.
26. Maste M.C.L., Rinia H.A., Brands C.M.J., Egmond M.R., Norde W. Proteolytic stability of Savinase in colloidal systems. Biochim. Biophys. Acta. 1252:1995;261-268.
27. de Jongh H.H.J., Goormaghtigh E., Killian A. Analysis of circular dichroism spectra of oriented protein-lipid complexes: toward a general application. Biochemistry. 33:1994;14521-14528.
28. Greenfield N., Fasman G.D. Computed circular dichroism spectra for evaluation of protein conformation. Biochemistry. 8:1969;4108-4116.
29. Chang C.T., Wu C.-S.C., Yang J.T. Circular dichroic analysis of protein conformation: inclusion of the β-turns. Anal. Biochem. 91:1978;13-31.
30. W.C. Johnson Jr., Circular dichroism instrumentation, in: G.D. Fasman (Ed.), Circular Dichroism and the Conformational Analysis of Biomolecules, Plenum Press, London, 1996, pp. 635-652.
31. Brock C.J., Enser M. A model system for studying protein binding to hydrophobic surfaces in emulsions. J. Sci. Food Agric. 40:1987;263-273.
32. Graham D.E., Phillips M.C. Proteins at liquid interfaces. II. Adsorption isotherms. J. Colloid Interface Sci. 70:1979;415-426.
33. P.E.A. Smulders, P.W.J.R. Caessens, P. Walstra, Emulsifying properties of β-casein and its hydrolysates in relation to their molecular properties, in: E. Dickinson (Ed.), Food Emulsions and Foams: Interfaces, Interactions and Stability, Royal Soc. Chem., Cambridge, 1998, in press.
34. Rost B., Sander C. Prediction of protein structure at better than 70% accuracy. J. Mol. Biol. 232:1993;584-594.
35. Rost B., Sander C. Combining evolutionary information and neutral networks to predict secondary structure. Proteins. 19:1994;55-72.
36. Rost B., Sander C., Schneider R. PHD - an automatic mail server for protein secondary structure prediction. CABIOS. 10:1994;53-60.
37. Chaplin L.C., Clark D.C., Smith L.J. The secondary structure of peptides derived from caseins: a circular dichroism study. Biochim. Biophys. Acta. 956:1988;162-172.
38. R.S. Bhatnagar, C.A. Gough, Circular dichroism of collagen and related polypeptides, in: G.D. Fasman (Ed.), Circular Dichroism and the Conformational Analysis of Biomolecules, Plenum Press, London, 1996, pp. 183-199.