Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-05T21:41:14.335Z Has data issue: false hasContentIssue false

Factors affecting the action of rennin in heated milk

Published online by Cambridge University Press:  01 June 2009

G. A. Wilson
Affiliation:
School of Biological Sciences, The University, Bradford, Yorkshire BD7 1DP
J. V. Wheelock
Affiliation:
School of Biological Sciences, The University, Bradford, Yorkshire BD7 1DP

Summary

The effect of temperature and time of heating whole milk on the renninclotting time, the primary phase of rennin action and the protein (mainly β-lactoglobulin) soluble in 2% trichloroacetic acid (TCA), have been studied. Considerable changes in these parameters occurred above 60°C. The primary phase was inhibited (the degree of inhibition being both temperature and time-dependent), the clotting time was increased, and the protein soluble in 2% TCA decreased considerably.

It is suggested that the inhibition of the primary phase was due to complex formation between κ-casein and β-lactoglobulin, the increase in clotting time to a combination of complex formation and a change in the distribution of Ca, and the decrease in β-lactoglobulin to both its interaction with κ-casein and its heat denaturation. The relevance of such changes to the heat stability of milk is discussed.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 1972

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Alais, C., Kiger, N. & Jollès, P. (1967). Journal of Dairy Science 50, 1738.Google Scholar
Briggs, D. R. & Hull, R. (1945). Journal of the American Chemical Society 67, 2007.CrossRefGoogle Scholar
Cherbuliez, E. & Baudet, P. (1950). Helvetica Chimica Acta 33, 1673.Google Scholar
Fox, K. K., Holsinger, V. H., Posati, L. P. & Pallansch, M. J. (1967). Journal of Dairy Science 50, 1363.Google Scholar
Hindle, E. J. & Wheelock, J. V. (1970 a). Journal of Dairy Research 37, 389.CrossRefGoogle Scholar
Hindle, E. J. & Wheelock, J. V. (1970 b). Journal of Dairy Research 37, 397.Google Scholar
Kannan, A. & Jenness, R. (1961). Journal of Dairy Science 44, 808.Google Scholar
Kresheck, G. C., Van Winkle, Q. & Gould, I. A. (1964). Journal of Dairy Science 47, 117.Google Scholar
Long, J. E., van Winkle, Q. & Gould, I. A. (1963). Journal of Dairy Science 46, 1329.Google Scholar
McKenzie, G. H., Norton, R. S. & Sawyer, W. H. (1971). Journal of Dairy Research 38, 343.Google Scholar
Mattick, E. C. V. & Hallett, H. S. (1929). Journal of Agricultural Science 19, 452.Google Scholar
Morrissey, P. A. (1969). Journal of Dairy Research 36, 333.Google Scholar
Pyne, G. T. (1953). Chemistry and Industry 72, 302.Google Scholar
Rose, D. (1963). Dairy Science Abstracts 25, 45.Google Scholar
Rose, D. (1965). Journal of Dairy Science 48, 139.CrossRefGoogle Scholar
Sawyer, W. H. (1969). Journal of Dairy Science 52, 1347.CrossRefGoogle Scholar
Tessier, H., Yaguchi, M. & Rose, D. (1969). Journal of Dairy Science 52, 139.Google Scholar
Wake, R. G. (1959). Australian Journal of Biological Sciences 12, 479.Google Scholar
Waugh, D. F. & Von Hippel, P. H. (1956). Journal of the American Chemical Society 78, 4576.Google Scholar
Zittle, C. A., Thompson, M. P., Custer, J. H. & Cerbulis, J. (1962). Journal of Dairy Science 45, 807.CrossRefGoogle Scholar