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The stability of milk protein to heat: I. Subjective measurement of heat stability of milk

Published online by Cambridge University Press:  01 June 2009

D. T. Davies  and
J. C. D. White
D. T. Davies
Affiliation:
The Hannah Dairy Research Institute, Ayr, Scotland
J. C. D. White
Affiliation:
The Hannah Dairy Research Institute, Ayr, Scotland
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Summary

A subjective test for the determination of the stability of milk protein to heat is described. In the test, the time required for particles of coagulated protein to become visible throughout a 2·5-ml sample of separated milk maintained at 135°C in a glass tube rocking at 8 c/min is taken as a measure of stability. The precision of the test was such that single determinations were generally adequate.

Coagulation time decreased by about 12% as rocking speed was increased over the range 4–12 c/min and increased by a factor of about 3 for a decrease in heating temperature of 10 degC over the range 140–105 °C; with some milks the Q10 °C value increased to 5–8 a temperature decreased. As sample volume was increased over the range 1–3 ml coagulation time increased, especially With milks whose coagulation was poor (initial clots small). This volume effect appeared to be a consequence of the accompanying decrease in the proportion of headspace oxygen to volume of milk.

Type
Original Articles
Information
Journal of Dairy Research , Volume 33 , Issue 1 , February 1966 , pp. 67 - 81
Copyright
Copyright © Proprietors of Journal of Dairy Research 1966

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References

REFERENCES

Belec, J. & Jenness, R. (1962). J. Dairy Sci. 45, 20.CrossRefGoogle Scholar
Blackburn, P. S., Laing, Constance M. & Malcolm, D. F. (1955). J. Dairy Res. 22, 37.CrossRefGoogle Scholar
Bruyne, N. A. de (1961). Res. Dev. Ind. (1), 94.Google Scholar
Cole, W. C. & Tarassuk, N. P. (1946). J. Dairy Sci. 29, 421.Google Scholar
Davies, J. M. (1959). 15th Int. Dairy Congr. 3, 1859.Google Scholar
Davies, D. T. & White, J. C. D. (1966). J. Dairy Res. 33, 83.Google Scholar
Finch, A. C. M. (1963). J. scient. Instrum. 40, 423.Google Scholar
Handbook of Chemistry and Physics (1947). 30th ed., p. 1978: Cleveland: Chemical Rubber Publishing Co.Google Scholar
Pyne, G. T. & McHenry, Kathleen A. (1955). J. Dairy Res. 22, 60.CrossRefGoogle Scholar
Rose, D. (1963). Review Article no. 190. Dairy Sci. Abstr. 25, 45.Google Scholar
Rose, D. & Tessier, H. (1959). J. Dairy Sci. 42, 969.CrossRefGoogle Scholar
Sommer, H. H. & Hart, E. B. (1919). J. biol. Chem. 40, 137.CrossRefGoogle Scholar
Sommer, H. H. & Hart, E. B. (1922). J. Dairy Sci. 5, 525.Google Scholar
Sommer, H. H. & Hart, E. B. (1926). Res. Bull. agric. Exp. Stn Univ. Wis. no. 67.Google Scholar
Webb, B. H. & Holm, G. E. (1932). J. Dairy Sci. 15, 345.Google Scholar
White, J. C. D. & Davies, D. T. (1958). J. Dairy Res. 25, 236.CrossRefGoogle Scholar
White, J. C. D. & Davies, D. T. (1966). J. Dairy Res. 33, 93.Google Scholar
Whitney, R. McL., Paulson, Katherine & Murthy, G. K. (1952). J. Dairy Sci. 35, 97.Google Scholar