Hostname: page-component-7bb8b95d7b-2h6rp Total loading time: 0 Render date: 2024-09-06T21:51:25.195Z Has data issue: false hasContentIssue false

Assessment of swine, bovine and chicken pepsins as rennet substitutes for Cheddar cheese-making

Published online by Cambridge University Press:  01 June 2009

Margaret L. Green
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9AT

Summary

Three enzymes were assessed as rennet substitutes for cheese-making. The bovine and chicken pepsins used were relatively crude extracts of bovine stomach mucosa and chicken proventriculae respectively; the swine pepsin was a partially purified commercial product. The ratios of milk-clotting activity to general proteolytic activity were high for rennet and bovine pepsin and low for swine and chicken pepsins. Both bovine mucosa and chicken stomach gave low milk-clotting activities compared with calf stomach. For all the enzymes the chemical reactions causing milk clotting appeared to be the same. The milk-clotting activity showed a decrease with increase in substrate pH for all the enzymes, although they were all still active at pH 6·81.

Duplicate cheeses were made from each of the swine, bovine and chicken pepsins, with rennet as a standard in each trial. The cheese-making process was similar with each enzyme, but differences appeared during ripening. The chicken-pepsin cheeses had poor body and weak Cheddar-cheese flavour, with many and intense off-flavours. The cheeses made with bovine and swine pepsins were only slightly inferior in quality and intensity of Cheddar-cheese flavour to the rennet cheeses. From a simulated cheese-making experiment it was concluded that 30–40 % of the added rennet, bovine pepsin and chicken pepsin was probably inactivated during the cheese-making process and that most or all of the swine pepsin was lost. These results provide an explanation for the variations observed in cheese ripening.

It was concluded that chicken pepsin would not prove a suitable rennet substitute for making Cheddar cheese because of the quality of the cheese produced, and that bovine pepsin would not prove suitable because of the cost of preparing a suitable extract. Swine pepsin would appear to be suitable if the ripening time were to be lengthened or if another enzyme were to be added to assist ripening; it is cheaper than rennet and other rennet substitutes.

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. (1963). Annls Biol. anim. Biochim. Biophys. 3, 65.CrossRefGoogle Scholar
Anderson, A. W. & Elliker, P. R. (1953). J. Dairy Sci. 36, 608.CrossRefGoogle Scholar
Antonini, J. & Ribadeau Dumas, B. (1971). Biochimie 53, 321.CrossRefGoogle Scholar
Berridge, N. J. (1945). Biochem. J. 39, 179.CrossRefGoogle Scholar
Berridge, N. J. (1952). Analyst, Lond. 77, 57.CrossRefGoogle Scholar
Berridge, N. J. (1955). Meth. Enzym. 2, 69.CrossRefGoogle Scholar
Bohak, Z. (1969). J. biol. Chem. 244, 4638.CrossRefGoogle Scholar
Burnett, J. & Scott Blair, G. W. (1963). Dairy Inds 28, 220.Google Scholar
Chapman, H. R. & Harrison, A. J. W. (1963). J. Soc. Dairy Technol. 16, 139.CrossRefGoogle Scholar
Cheeseman, G. C. (1968). J. Dairy Res. 35, 439.CrossRefGoogle Scholar
Davies, D. T. & White, J. C. D. (1960). J. Dairy Res. 27, 171.CrossRefGoogle Scholar
Davis, J. G. (1971). Dairy Inds 36, 135.Google Scholar
Ernstrom, C. A. (1961). Milk Prod. J. 52 (5), 8.Google Scholar
Foltmann, B. (1966). C. r. Trav. Lab. Carlsberg 35, 143.Google Scholar
Fox, P. F. (1969). J. Dairy Res. 36, 427.CrossRefGoogle Scholar
Herriott, R. M. (1955). Meth. Enzym. 2, 3.CrossRefGoogle Scholar
Itzhaki, R. F. & Gill, D. M. (1964). Analyt. Biochem. 9, 401.CrossRefGoogle Scholar
Kizer, D. E., Hankin, L., Speck, M. L. & Aurand, L. W. (1955). J. Dairy Sci. 38, 303.CrossRefGoogle Scholar
Kushner, I., Rapp, W. & Burtin, P. (1964). J. clin. Invest. 43, 1983.CrossRefGoogle Scholar
Lang, C. A. (1958). Analyt. Chem. 30, 1692.CrossRefGoogle Scholar
Maragoudakis, M. E., Young, J. O. & Stein, R. W. (1961). J. Dairy Sci. 44, 2339.Google Scholar
Melachouris, N. P. & Tuckey, S. L. (1964). J. Dairy Sci. 47, 1.CrossRefGoogle Scholar
Naudts, M. (1969). Int. Dairy Fed. a. Bull. (7) 1.Google Scholar
Prentice, J. H. (1954). Lab. Pract. 3, 186.Google Scholar
Prins, J. & Nielsen, T. K. (1970). Process Biochem. 5 (5), 34.Google Scholar
Reps, A., Poznański, S. & Kowalska, W. (1970). Milchwissenschaft 25, 146.Google Scholar
Sardinas, J. L. (1969). Process Biochem. 4 (7), 13.Google Scholar
Schulz, M. E. & Thomasow, J. (1970). 18th Int. Dairy Congr., Sydney 1 E, 321.Google Scholar
Taylor, W. H. (1968). In Handbook of Physiology, section 6, vol. 5, p. 2567. (Ed. Code, C. F..) Washington, D.C.: Am. Physiol. Soc.Google Scholar