Hostname: page-component-78c5997874-t5tsf Total loading time: 0 Render date: 2024-11-19T08:16:52.020Z Has data issue: false hasContentIssue false
  • English
  • Français

Denaturation of porcine pepsin during Cheddar cheese manufacture

Published online by Cambridge University Press:  01 June 2009

A. M. O'Keeffe ,
P. F. Fox  and
C. Daly
A. M. O'Keeffe
Affiliation:
Departments of Food Chemistry and Microbiology, University College, Cork, Irish Republic
P. F. Fox
Affiliation:
Departments of Food Chemistry and Microbiology, University College, Cork, Irish Republic
C. Daly
Affiliation:
Departments of Food Chemistry and Microbiology, University College, Cork, Irish Republic
Get access Rights & Permissions [Opens in a new window]

Summary

Porcine pepsin was rapidly denatured in phosphate buffers, pH 6·4–6·7, in the temperature range 31–39 °C and was only slightly more stable in milk under similar conditions. However, the enzyme was considerably more stable in Cheddar cheese curd in which the extent of denaturation was very markedly influenced by the pH of the milk at setting. Under normal cheese-making conditions, porcine pepsin was about equally stable with chymosin. Two modifications of the cheesemanufacturing procedure were developed which permit the manufacture of cheese almost free of coagulant and suitable for the assessment of the contribution of starter proteinases to proteolysis during cheese ripening.

Type
Original Articles
Information
Journal of Dairy Research , Volume 44 , Issue 2 , June 1977 , pp. 335 - 343
Copyright
Copyright © Proprietors of Journal of Dairy Research 1977

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

Cheryan, M., van Wyk, P. J., Olson, N. F. & Richardson, T. (1975). Journal of Dairy Science 58, 477.CrossRefGoogle Scholar
Fox, P. F. (1969). Journal of Dairy Research 36, 427.CrossRefGoogle Scholar
Green, M. L. (1972). Journal of Dairy Research 39, 261.CrossRefGoogle Scholar
Green, M. L. & Foster, P. M. D. (1974). Journal of Dairy Research 41, 269.CrossRefGoogle Scholar
Herriott, R. M. (1955). Methods in Enzymology 2, 3.CrossRefGoogle Scholar
Holmes, D. G. & Ernstrom, C. A. (1973). Journal of Dairy Science 56, 622, 623.Google Scholar
Ledford, R. A., O'Sullivan, A. C. & Nath, K. R. (1966). Journal of Dairy Science 49, 1089.Google Scholar
Melachouris, N. P. & Tuckey, S. L. (1964). Journal of Dairy Science 47, 1.Google Scholar
O'Keeffe, R. B., Fox, P. F. & Daly, C. (1975). Journal of Dairy Research 42, 111.CrossRefGoogle Scholar
O'Keeffe, R. B., Fox, P. F. & Daly, C. (1976). Irish Journal of Agricultural Research 15, 151.Google Scholar
O'Leary, P. A. & Fox, P. F. (1974). Journal of Dairy Research 41, 381.CrossRefGoogle Scholar
Thompson, M. P., Kiddy, C. A., Johnston, J. O. & Wienberg, R. M. (1964). Journal of Dairy Science 47, 378.CrossRefGoogle Scholar
Visser, F. M. W. (1976). Netherlands Milk and Dairy Journal 30, 41.Google Scholar