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The kinetics of the rennin-casein reaction in abnormal cow's milk and milks of some other species and of the action of rennet substitutes on normal cow's milk

Published online by Cambridge University Press:  01 June 2009

J. C. Oosthuizen
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading

Summary

In earlier papers it was shown that the fall in viscosity of milk and caseinate solutions acted on by rennet, follows a first-order reaction equation. The reaction rate constant has been found to be independent of the source of the caseinate substrate used. This seems to be true not only for caseinate from normal cow's milk but also from colostrum, slow-clotting cow's milk and even the milk of buffaloes, sheep and probably goats.

With solutions of caseinate from sow's milk the reaction kinetics and the proportional viscosity loss were similar to those of cow's caseinate but the rate constants were much lower. Rennet showed no measurable reaction with human, whale, mare or rhinoceros caseinates but produced a constant rate of fall in the viscosity of a camel caseinate for more than an hour from rennetting.

Vegetable and microbiological rennet substitutes also produce a fall in the viscosity of sodium caseinate and the reactions follow first-order kinetics. They differ from cheese rennet in that the proteolysis involved is stronger and is not as limited as that of rennin since they attack at least twice as much of the casein ensemble. This might suggest a mixture of enzymes but since the proportionality between enzyme concentration and k1 was very close this seems unlikely.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1962

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References

REFERENCES

Aschaffenburg, R., Gregory, M. E., Rowland, S. J., Thompson, S. Y. & Kon, V. M. (1961). Proc. zool. Soc. Lond. 137, 475.Google Scholar
Berridge, N. J. (1954). In Advanc. Enzymol. 15, 423.Google Scholar
Chevalier, R., Mocquot, G., Alais, C. & Bonnat, M. (1950 a). C.R. Acad. Sci., Paris, 230, 581.Google Scholar
Chevalier, R., Mocquot, G., Alais, C. & Bonnat, M. (1950 b). C.R. Acad. Sci., Paris, 231, 249.Google Scholar
Garnier, J. (1957). Ann. Tech. agric. 3, 245.Google Scholar
Graber, H. T. (1917). Industr. Engng Chem. 9, 1125.CrossRefGoogle Scholar
Hostettler, H. & Rüegger, H. R. (1950). Landw. Jb. Schweiz, 64, 669.Google Scholar
Krishnaswamy, M. A., Johar, D. S., Subrahmanyan, V. & Thomas, S. P. (1961). Food Tech., Champaign, 15, 482.Google Scholar
Pyne, G. T. (1953). Chem. & Ind. p. 302.Google Scholar
Pyne, G. T. (1955). Dairy Sci. Abstr. 17, 532.Google Scholar
Scott Blair, G. W. & Oosthuizen, J. C. (1961 a). J. Dairy Res. 28,165.CrossRefGoogle Scholar
Scott Blair, G. W. & Oosthuizen, J. C. (1961 b). Nature, Lond., 191, 697.Google Scholar
Scott Blair, G. W. & Oosthuizen, J. C. (1962). J. Dairy Res. 29, 37.CrossRefGoogle Scholar
Stevenson, C. (1917). J. Agric. (N.Z.) 14, 32.Google Scholar
Tsugo, T. & Yamauchi, K. (1959). Proc. 15th Int. Dairy Congr. 2, 636, 643.Google Scholar
Van Dam, W. (1915). Versl. Landbouwk. Onderzoek, 18, 147.Google Scholar
Veringa, H. A. (1961). Dairy Sci. Abstr. 23, 197.Google Scholar