Advertisement

The Formation and Stabilisation of Protein Foams

  • D. C. Clark
  • M. Coke
  • L. J. Smith
  • D. R. Wilson
Part of the Springer Series in Applied Biology book series (SSAPPL.BIOLOGY)

Abstract

Protein foams play an important role in many processes in the beverage and food industries and this has stimulated interest in their formation and stability. Population of the air/water interface by protein molecules involves an adsorption process, which is diffusion controlled, followed by a conformational change, often referred to as surface denaturation (Graham and Phillips 1979a, b, c). These processes are the subject of considerable investigation in order to gain insight into the mechanism of foam stabilisation, with the long term objective of defining rules which allow prediction and improvement of the behaviour of existing molecules and the design of new surface active proteins and peptides.

Keywords

Sodium Dodecyl Sulphate Circular Dichroism Fluorescence Recovery After Photobleaching Interlamellar Space Protein Film 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Axelrod D, Koppel DE, Schlessinger J, Elson E, Webb W (1976) Mobility measurements by analysis of fluorescence photobleaching recovery kinetics. Biophys J 16:1055–1069CrossRefGoogle Scholar
  2. Bacon JR, Hemmant JW, Moore R, Wright DJ (1988) Characterisation of the foaming properties of lysozymes and α-lactalbumin: a structural evaluation. Food Hydrocolloid 2:225–245CrossRefGoogle Scholar
  3. Beck K, Peters R (1985) Translational diffusion and phase separation in phospholipid monolayers: A fluorescence microphotolysis study. In: Bayley PM, Dale RE (eds) Spectroscopy and the dynamics of molecular biological systems. Academic Press, London, pp 177–196Google Scholar
  4. Beechem JM, Brand L (1985) Time resolved fluorescence of proteins. Ann Rev Biochem 54:43–71CrossRefGoogle Scholar
  5. Bell K, McKenzie HA, Murphy WH, Shaw DC (1970) A comparison of bovine α-lactalbumin A and B of Droughtmaster. Biochim Biophys Acta 214:437–444CrossRefGoogle Scholar
  6. Boyd J, Sherman P (1970) Two-dimensional rheological studies on surfactant films at interfaces. J Colloid Interface Sci 34:76–80CrossRefGoogle Scholar
  7. Boyd J, Mitchell JR, Irons L, Musselwhite PR, Sherman P (1973) The mechanical properties of milk protein films spread at the air-water interface. J Colloid Interface Sci 45:478–486CrossRefGoogle Scholar
  8. Clark DC, Coke M, Mackie AR, Pinder AC, Wilson DR (1989a) Molecular diffusion and thickness measurements of protein stabilised thin films. J Colloid Interface Sci (submitted Feb 1989)Google Scholar
  9. Clark DC, Dann R, Mackie AR, Mingins J, Pinder AC, Purdy PW, Russell EJ, Smith LJ, Wilson DR (1989b) Surface diffusion in sodium dodecyl sulphate stabilised thin films. Langmuir (submitted Mar 1989)Google Scholar
  10. Clark DC, Mackie AR, Smith LJ, Wilson DR (1989c) Electrostatic interactions between proteins and their effect on foam composition and stability In: Bee RD, Mingins J, Richmond P (eds) Food colloids. Royal Society of Chemistry special publication no. 58. London, in pressGoogle Scholar
  11. Daniel E, Weber G (1966) Co-operative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalene sulphonate. Fluorimetric titrations. Biochemistry 6:1893–1900CrossRefGoogle Scholar
  12. Dickinson E, Murray BS, Stainsby G (1985) Time dependent surface viscosity of adsorbed films of casein and gelatin at the oil water interface. J Colloid Interface Sci 106:259–262CrossRefGoogle Scholar
  13. Eberhart RC, Munro MS, Frautschi JR, Sevastianov VI (1987) In: Brash JL, Horbett TA (eds) Proteias at interfaces: physicochemical and biochemical studies, vol 343. American Chemical Society, Washington DC, USA, pp 378–400CrossRefGoogle Scholar
  14. Enser M, Clark DC (1988) In: AFRC Institute of Food Research Annual Report 1988, pp 52-53Google Scholar
  15. Exerowa D, Kolarov T, Khristov K (1987) Direct measurement of disjoining pressure in black foam films. 1. Films from an anionic surfactant. Colloids Surf 22:171–185Google Scholar
  16. Gendreau RM, Leininger RI, Winters S, Jakobsen RJ (1982) Fourier-transform infra-red spectroscopy for protein surface studies. In: Cooper SL, Peppas NA (eds) Biomaterials: interfacial phenomena and applications, vol 199. American Chemical Society, Washington DC, USA, pp 371-379Google Scholar
  17. Graham ARB, Malcolm GN, McKenzie HA (1984) On the isolation and conformation of β-casein A. Intl J Biol Macromol 6:155–161CrossRefGoogle Scholar
  18. Graham DE, Phillips MC (1976) The conformation of proteins at the air/water interface. In: Akers RJ (ed) Foams. Academic Press, New York, pp 75–98Google Scholar
  19. Graham DE, Phillips MC (1979a) Protein at liquid interfaces. I. Kinetics of adsorption and surface denaturation. J Colloid Interface Sci 70:403–414CrossRefGoogle Scholar
  20. Graham DE, Phillips MC (1979b) Protein at liquid interfaces. II. Adsorption isotherms. J Colloid Interface Sci 70:415–426CrossRefGoogle Scholar
  21. Graham DE, Phillips MC (1979c) Protein at liquid interfaces. III. Molecular structures of adsorbed films. J Colloid Interface Sci 70:427–439CrossRefGoogle Scholar
  22. Halford SE (1975) Stopped-flow fluorescence studies on saccharide binding to lysozyme. Biochem J 149:411–422Google Scholar
  23. Hailing PJ (1981) Protein stabilised foams and emulsions. CRC Crit Rev Food Sci Nutri 155-203Google Scholar
  24. Inokuchi K (1955) Rheology of surface films. I. Rheological characteristics of monomolecular films of ovalbumin and serum albumin. Bull Chem Soc (Japan) 26:500–507CrossRefGoogle Scholar
  25. James LK, Sherman P (1976) Creep compliance studies of egg yolk lipoprotein interfacial films. In: Biorheology, vol 13. Pergamon Press, Oxford, England, pp 79–81Google Scholar
  26. Johnson WC (1988) Secondary structure of proteins through circular dichroism spectroscopy. Ann Rev Biophys Biophys Chem 17:145–166CrossRefGoogle Scholar
  27. Konno T, Meguro H, Tuzimura K (1975) D-pantolactone as a circular dichroism (CD) calibration. Analyt Biochem 67:226–232CrossRefGoogle Scholar
  28. McMillin CR, Walton AG (1974) A circular dichroism technique for the study of adsorbed protein. J Colloid Interface Sci 48:345–349CrossRefGoogle Scholar
  29. Musselwhite PR, Kitchener JA (1967) The limiting thickness of protein films. J Colloid Interface Sci 24:80–83CrossRefGoogle Scholar
  30. Pinder AC, Clark DC (1986) Beyond the fringe: Total internal reflection spectroscopy. Lab Practice 36:45–49Google Scholar
  31. Provencher SW, Glockner J (1981) Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20:33–37CrossRefGoogle Scholar
  32. Takakuwa T, Konno T, Meguro H (1985) A new standard substance for calibration of circular dichroism: Ammonium d-10-camphor sulphonate. Analyt Sci 1:215–218CrossRefGoogle Scholar
  33. Walton AG, Koltisko B (1982) Protein structure and the kinetics of interaction with surfaces. In: Cooper SL, Peppas NA (eds) Biomaterials: interfacial phenomena and applications, vol 199. American Chemical Society, Washington DC, USA, pp 245–264Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1989

Authors and Affiliations

  • D. C. Clark
  • M. Coke
  • L. J. Smith
  • D. R. Wilson

There are no affiliations available

Personalised recommendations