Hostname: page-component-848d4c4894-2xdlg Total loading time: 0 Render date: 2024-06-16T14:55:18.366Z Has data issue: false hasContentIssue false

Quantification of milk-clotting enzymes in 40 commercial bovine rennets, comparing rocket immunoelectrophoresis with an activity ratio assay

Published online by Cambridge University Press:  01 June 2009

G. A. L. Rothe
Affiliation:
Research Department of Chr. Hansen's Laboratory, Sankt Annœ Plads 3, DK-1250 Copenhagen K, Denmark
M. K. Harboe
Affiliation:
Research Department of Chr. Hansen's Laboratory, Sankt Annœ Plads 3, DK-1250 Copenhagen K, Denmark
S. C. Martiny
Affiliation:
Research Department of Chr. Hansen's Laboratory, Sankt Annœ Plads 3, DK-1250 Copenhagen K, Denmark

Summary

The enzymes chymosin, bovine pepsin A and bovine pepsin B in 40 commercial rennets were assayed by rocket immunoelectrophoresis, using monospecific antibody preparations against the 3 enzymes. Concentrations found were chymosin, 0–1208 mg/l; bovine pepsin A, 359–3818 mg/l; bovine pepsin B, 0–320 mg/l. Bovine pepsin B was found to be a minor enzymic component in bovine rennets, representing maximally 2·9 % of the milk-clotting activity or 9·7 % of the weight of the enzymes. The sensitivity for the quantification of the 3 enzymes was 0·5–1·0 mg/l. The coefficient of variation was 3·7 %. The sum of the immunochemical data converted into milk-clotting activities was in good agreement with the directly observed milk-clotting activity, indicating that there was no immunochemical overestimation due to the presence of non-enzymic active antigens. A high correlation was found between the enzymic composition determined immunochemically and by activity ratio assay.

Type
Original Articles
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

Antonini, J. & Ribadeau Dumas, B. (1971). Biochimie 53, 321.CrossRefGoogle Scholar
Foltmann, B. (1970). Methods in Enzymology 19, 421.CrossRefGoogle Scholar
Garnot, P., Thapon, J. L., Mathieu, C. M., Maubois, J. L. & Ribadeau Dumas, B. (1972). Journal of Dairy Science 55, 1641.CrossRefGoogle Scholar
Harboe, M., Andersen, P. M., Foltmann, B., Kay, J. & Kassell, B. (1974). Journal of Biological Chemistry 249, 4487.CrossRefGoogle Scholar
Harboe, N. & Ingild, A. (1973). Scandinavian Journal of Immunology 2, Suppl. No. 1, 161.CrossRefGoogle Scholar
Rothe, G. A. L., Axelsen, N. H., Jøhnk, P. & Foltmann, B. (1976). Journal of Dairy Research 43, 85.CrossRefGoogle Scholar