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Detection of residual chymosin in cheese by an enzyme-linked immunosorbent assay

Published online by Cambridge University Press:  01 June 2009

Nissab Boudjellab ,
Odile Rolet-Repecaud  and
Jean-Claude Collin
Nissab Boudjellab
Affiliation:
INRA, Station de Recherches en Technologie et Analyses Laitières, BP 89, 39801 Poligny, France
Odile Rolet-Repecaud
Affiliation:
INRA, Station de Recherches en Technologie et Analyses Laitières, BP 89, 39801 Poligny, France
Jean-Claude Collin
Affiliation:
INRA, Station de Recherches en Technologie et Analyses Laitières, BP 89, 39801 Poligny, France
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Summary

A simple and rapid competitive enzyme-linked immunosorbent assay method has been developed to detect the residual activity of chymosin in various types of cheese without extraction. In a cheese of the Saint-Paulin type, concentrations of chymosin detected at the end of cheesemaking in curd and whey represented 22·5 and 73·5% respectively of the total amount added to milk, so most of the chymosin was detected using this method. In a cooked pressed cheese of the Comté type, only 14% of the chymosin added to milk was detected in curd and all the chymosin in whey was inactivated. It was thus possible to demonstrate the presence of active residual chymosin in cooked pressed cheese. When measurements were carried out in 12 different cheeses, chymosin concentrations ranged between 384 ng/g in a Camembert cheese and 86 ng/g for an 8-month old Comté cheese. Chymosin appeared to be highly stable during cheese ripening.

Type
Original Articles
Information
Journal of Dairy Research , Volume 61 , Issue 1 , February 1994 , pp. 101 - 109
Copyright
Copyright © Proprietors of Journal of Dairy Research 1994

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References

REFERENCES

Andersson, H., Andrén, A. & Björck, L. 1989 An enzyme-linked immunogrsorbent assay for detection of Chymosin in dairy products. Journal of Dairy Science 72 3129–3133CrossRefGoogle Scholar
Andren, A., Dekoning, P. J. & Björck, L. 1983 Changes in immunologically and catalytically active sites of chymosin, bovine pepsin and porcine pepsin. Netherlands Milk and Dairy Journal 37 11–20Google Scholar
Avrameas, S. 1969 Coupling of enzymes to proteins with glutaraldehyde. Use of the conjugates for the detection of antigens and antibodies. Immunochemistry 6 43–52CrossRefGoogle ScholarPubMed
Collin, J. C., Compagnone, P., Ryba, I. & Baer, A. 1988 Determination of plasmin (alkaline milk proteinase) and chymosin in milk products by the ELISA assay. Lait 68 235–239CrossRefGoogle Scholar
Collin, J. C., Grappin, R. & Legraet, Y. 1977 [Study of Berridge's method for the determination of milk coagulation time by rennet.] Revue Laitière Française no. 355 389, 391–394Google Scholar
Collin, J. C., Martin, P., Garnot, P., Ribadeau Dumas, B. & Mocquot, G. 1981 Determination of chymosin and bovine pepsine A in commercial bovine rennets and pepsins. Milchwissenchaft 36 32–35Google Scholar
Elliott, J. A. & Emmons, D. B. 1971 Rennin detection in cheese with the passive indirect hemagglutination test. Canadian Institute of Food Technology Journal 4 16–18CrossRefGoogle Scholar
Garnot, P. 1985 Heat-stability of milk-clotting enzymes. Technological consequences. International Dairy Federation Bulletin Document 194 2–7Google Scholar
Garnot, P. & Martin, P. 1979 [Rennet: composition, determination of its activity and its role in the cheese factory.] Technique Laitière no. 930 27–30Google Scholar
Garnot, P., Thapon, J. L., Mathieu, C. M., Maubois, J. L. & Ribadeau Dumas, B. 1972 Determination of rennin and bovine pepsins in commercial rennets and abomasal juices. Journal of Dairy Science 55 1641–1650CrossRefGoogle Scholar
Gripon, J. C., Demazeaud, M. J., Le Bars, D. & Bergère, J. L. 1975 [Study of the role of microorganisms and enzymes during the ripening of cheeses. II. Influence of commercial rennet.] Lait 55 502–516CrossRefGoogle Scholar
Holmes, D. G., Duersch, J. W. & Ernstrom, G. A. 1977 Distribution of milk clotting enzymes between curd and whey and their survival during Cheddar cheese making. Journal of Dairy Science 60 862–869CrossRefGoogle Scholar
International Dairy Federation 1987 Calf rennet and adult bovine rennet. Determination of chymosin and bovine pepsin contents (Chromatographie method). IDF Standard no. 110AGoogle Scholar
Klostermeyer, H., Thomasow, J. & Wiechen, A. 1972 [A method for studying rennet distribution in whey and curd using rennin labelled with 131I.] Milchwissenchaft 27 102–106Google Scholar
Lawrence, R. C. & Sanderson, W. B. 1969 A micro-method for the quantitative estimation of rennets and other proteolytic enzymes. Journal of Dairy Research 36 21–29CrossRefGoogle Scholar
Matheson, A. R. 1981 The immunochemical determination of chymosin aetivity in cheese. New Zealand Journal of Dairy Science and Technology 16 33–41Google Scholar
Stadhouders, J., Hup, G. & Van Der Waals, C. B. 1977 Determination of calf rennet in cheese. Netherlands Milk and Dairy Journal 31 3–15Google Scholar
Taniguchi, K., Tsuji, H., Kojima, I., Kasamoto, K. & Minamisako, K. 1987 [Determination of chymosin in cheese by enzyme immunoassay.] Bulletin of the Faculty of Agriculture, Meiji University no. 76 1–27Google Scholar