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The effect of the chemical structure of additives on the coagulation of casein micelle suspensions by rennet

Published online by Cambridge University Press:  01 June 2009

Richard J. Marshall  and
Margaret L. Green
Richard J. Marshall
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9 AT
Margaret L. Green
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9 AT
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Summary

Casein micelles in milk-salts solution adsorbed charged detergents and highly-charged polypeptides strongly, neutral detergents less strongly and low molecular-weight amines weakly. A tetra-amine was adsorbed more strongly than a tri-amine. The extent of adsorption of proteins tended to rise as the molecular weight increased. Glycerol and lactate were adsorbed to a limited extent but dextran and α-ketoglutarate were not adsorbed at all. Proline was partly adsorbed, indicating that hydrophobic binding sites were available, and caused some disruption of the casein micelles. Additives were bound to approximately the same extent by casein micelles and rennet coagula. The proportions adsorbed were constant over at least 10-fold ranges of concentration. Additives which increased the rennet clotting time (RCT) acted by binding Ca2+. Most additives decreased the RCT, the extent increasing with the amount adsorbed and the positive charge on the additive. The greatest reduction in RCT was observed with those additives which had positively-charged and hydrophobic moieties and bound most strongly to casein micelles. Of the additives tested, only sodium dodecyl sulphate affected the enzymic action of rennet. The reduction in RCT may have resulted from the neutralization of the negative charge of the micelles or enhancement of their hydrophobicity, favouring hydrophobic interactions between the particles.

Type
Original Articles
Information
Journal of Dairy Research , Volume 47 , Issue 3 , October 1980 , pp. 359 - 369
Copyright
Copyright © Proprietors of Journal of Dairy Research 1980

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References

REFERENCES

Anfinsen, C. B., Redfield, R. R., Choate, W. L., Page, J., & Carroll, W. R. (1954). Journal of Biological Chemistry 207, 201–210.Google Scholar
Barker, S. B. & Summerson, W. H. (1941). Journal of Biological Chemistry 138, 535–554.Google Scholar
Barratt, M. D., Austin, J. P. & Whitehurst, R. J. (1974). Biochimica et Biophysica Acta 348, 126–135.CrossRefGoogle Scholar
Barratt, M. D. & Rayner, L. (1972). Biochimica et Biophysica Acta 255, 974–980.Google Scholar
Beschetnova, E. T., Golovina, A. P. & Zorov, N. B. (1973). Zhurnal Analiticheskoi Khimii 28, 1943. See Analytical Abstracts 28, 508 (1975).Google Scholar
Browne, W. J., North, A. C. T., Phillips, D. C., Brew, K., Vanaman, T. C. & Hill, R. L. (1969). Journal of Molecular Biology 42, 65–86.Google Scholar
Castle, A. V. & Wheelock, J. V. (1972). Journal of Dairy Research 39, 15–22.CrossRefGoogle Scholar
Ceriotti, G. (1971). Clinical Chemistry 17, 400–402.CrossRefGoogle Scholar
Chaplin, B. & Green, M. L. (1980). Journal of Dairy Research 47, 351–358.Google Scholar
Cheeseman, G. C. (1968). Journal of Dairy Research 35, 439–446.CrossRefGoogle Scholar
Cheeseman, G. C. & Jeffcoat, J. (1970). Journal of Dairy Research 37, 245–257Google Scholar
Cheeseman, G. C. & Knight, D. (1970). Journal of Dairy Research 37, 259–267.Google Scholar
Dalgleish, D. G. (1973). European Journal of Biochemistry 40, 375–380.Google Scholar
Dickerson, R. E. & Timkovich, R. (1975). In The Enzymes, 3rd edn, vol. IIa, pp. 397–547. (Ed. Boyer, P. D..) New York: Academic Press.Google Scholar
Dickson, I. R. & Perkins, D. J. (1971). Biochemical Journal 124, 235–240.Google Scholar
Dirsoherl, W. & Dohr, H. (1974). Hoppe-Seyler's Zeitschrift für Physiologische Chemie 355, 1135–1138.Google Scholar
Green, M. L. & Crutchfield, G. (1969). Biochemical Journal 115, 183–190.CrossRefGoogle Scholar
Green, M. L. & Crutchfield, G. (1971). Journal of Dairy Research 38, 151–164.Google Scholar
Green, M. L. & Marshall, R. J. (1977). Journal of Dairy Research 44, 521–531.Google Scholar
Green, M. L. & Marshall, R. J. (1979). Journal of Dairy Research 46, 365–367.CrossRefGoogle Scholar
Gregory, G. R. E. C. (1966). Analyst 91, 251–257.CrossRefGoogle Scholar
Hillier, R. M. (1976). Journal of Dairy Research 43, 259–265.Google Scholar
Ho, C. & Waugh, D. F. (1965a). Journal of the American Chemical Society 87, 110–117.CrossRefGoogle Scholar
Ho, C. & Waugh, D. F. (1965b). Journal of the American Chemical Society 87, 889–892.Google Scholar
Lee, J. C., Gekko, K. & Timasheff, S. N. (1979). Methods in Enzymology 61, 26–49.Google Scholar
Lyster, R. L. J. (1972). Journal of Dairy Research 39, 279–318.Google Scholar
Mcintire, F. C., Roth, L. W. & Shaw, J. L. (1947). Journal of Biological Chemistry 170, 537–544.CrossRefGoogle Scholar
Mckenzie, H. A. (1971). In Milk Proteins, vol. 2, pp. 257–330. (Ed. McKenzie, H. A..) New York: Academic pressCrossRefGoogle Scholar
Margoliash, E. & Smith, E. L. (1961). Nature 192, 1121–1123.Google Scholar
Mokrasch, L. C. (1967). Analytical Biochemistry 18, 64–71.Google Scholar
Neuberger, A. & Marshall, R. D. (1966). In Glycoproteins, pp. 299–316. (Ed. Gottschalk, A..) Amsterdam: Elsevier Publishing Co.Google Scholar
Oginsky, E. L. (1957). Methods in Enzymology 3, 639–643.Google Scholar
Ough, C. S. (1969). Journal of Food Science 34, 228–230.Google Scholar
Paléus, S. & Paul, K. G. (1963). In The Enzymes, 2nd edn, vol. 8, pp. 97–112. (Ed. Boyer, P. D..) New York: Academic Press.Google Scholar
Payens, T. A. J. (1966). Journal of Dairy Science 49, 1317–1324.CrossRefGoogle Scholar
Payens, T. A. J. (1977). Biophysical Chemistry 6, 263–270.Google Scholar
Pearce, K. N. (1976). Journal of Dairy Research 43, 27–36.Google Scholar
Pyne, G. T. (1962). Journal of Dairy Research 29, 101–130.CrossRefGoogle Scholar
Pyne, G. T. & Mcgann, T. C. A. (1960). Journal of Dairy Research 27, 9–17.CrossRefGoogle Scholar
Schobert, B. & Tschesche, H. (1978). Biochimica et Biophysica Acta 541, 270–277.Google Scholar
Sheiham, I. & Pinfold, T. A. (1969). Analyst 94, 387–388.Google Scholar
Slein, M. W. & Logan, G. F. (1956). Biochimica et Biophysica Acta 20, 118–128.Google Scholar
Smyth, D. G., Stein, W. H. & Moore, S. (1963). Journal of Biological Chemistry 238, 227–234.CrossRefGoogle Scholar
Snoeren, T. H. M., Payens, T. A. J., Jeunink, J. & Both, P. (1975). Milchwissenschaft 30, 393–396.Google Scholar
Spiro, R. G. (1966). Methods in Enzymology 8, 3–26.Google Scholar
Stevenson, D. G. (1954). Analyst 79, 504–507.Google Scholar
Tanford, C. & Roxby, R. (1972). Biochemistry 11, 2192–2198.CrossRefGoogle Scholar
Tarassuk, N. P. & Richardson, G. A. (1941). Journal of Dairy Science 24, 667–677.Google Scholar
White, I. G. (1959). Australian Journal of Experimental Biology and Medical Science 37, 441–450.CrossRefGoogle Scholar
Zittle, C. A. & Custer, J. H. (1963). Journal of Dairy Science 46, 1183–1188.CrossRefGoogle Scholar