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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
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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

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References

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