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α-Amylase in whole egg and its sensitivity to pasteurization temperatures

Published online by Cambridge University Press:  15 May 2009

J. Brooks
J. Brooks
Affiliation:
Low Temperature Research Station, Downing Street, Cambridge
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The activity of the enzyme α-amylase of whole egg is known to be sensitive to pasteurizing temperatures and the possibility that this property could be used as a control test for the adequacy of pasteurization has been examined.

The occurrence of the enzyme, the physico-chemical characteristics of its heat inactivity, the consistency of its behaviour in large numbers of eggs and the influence on its of packing station procedures has been studied.

By sampling eggs from many sources for 11 months it was concluded that the activity of the enzyme was consistent, the inactivation by heat was a first-order reaction, and freezing, thawing, homogenization, spray-drying and in the laboratory freeze-drying did not affect its inactivation. But there was some interference from added citrate and sucrose.

Type
Research Article
Information
Journal of Hygiene , Volume 60 , Issue 2 , June 1962 , pp. 145 - 151
Copyright
Copyright © Cambridge University Press 1962

References

REFERENCES

Aschaffenburg, R. & Mullen, J. E. C. (1949). J. Dairy Res. 16, 58.CrossRefGoogle Scholar
Association of Official Agricultural Chemists (1955). Official Methods of Analysis of Association of Official Agricultural Chemists. 8th edn.Washington 4, D.C.Google Scholar
Botham, G. H. (1952). Mon. Bull. Minist. Hlth Lab. Serv. 11, 82.Google Scholar
Brooks, J. & Taylor, D. J. (1955). Food Invest. Spec. Rep. No. 60. London: H.M. Stationery Office.Google Scholar
Eddy, B. P. (1958). Antonie van Leeuwenhoek, 24, 81.CrossRefGoogle Scholar
Heller, C. L., Roberts, G. B. C., Amos, A. J., Smith, M. E. & Hobbs, B. C. (1962). J. Hyg., Camb., 60, 135.CrossRefGoogle Scholar
Kästli, P. (1957). Dairy Sci. Abstr. 19, 784.Google Scholar
Kay, H. D. & Graham, W. R. Jr., (1935). J. Dairy Res. 6, 191.CrossRefGoogle Scholar
Koga, T. (1923). Biochem. Z. 141, 430.Google Scholar
Lineweaver, H., Morris, H. J., Kline, L. & Bean, R. S. (1948). Arch. Biochem. 16, 443.Google Scholar
Murdock, C. R., Crossley, E. L., Robb, J., Smith, M. E. & Hobbs, B. C. (1960). Mon. Bull. Minist. Hlth Lab. Serv. 19, 134.Google Scholar
van Oijen, C. F. (1940). Tijdschr. Diergeneesk. 67, 686.Google Scholar
Schormüller, J. & Hothorn, S. (1956). Dtsch. LebensmittRdsch. 52, 57.Google Scholar