Hostname: page-component-78c5997874-t5tsf Total loading time: 0 Render date: 2024-11-02T22:15:32.618Z Has data issue: false hasContentIssue false
  • English
  • Français

Milk enzymes—their distribution and activity

Published online by Cambridge University Press:  01 June 2009

B. J. Kitchen ,
G. C. Taylor  and
I. C. White
B. J. Kitchen
Affiliation:
Otto Madsen Dairy Research Laboratory, Harbour Road, Hamilton, Brisbane, 4007, Australia
G. C. Taylor
Affiliation:
Otto Madsen Dairy Research Laboratory, Harbour Road, Hamilton, Brisbane, 4007, Australia
I. C. White
Affiliation:
Otto Madsen Dairy Research Laboratory, Harbour Road, Hamilton, Brisbane, 4007, Australia
Get access Rights & Permissions [Opens in a new window]

Summary

The distribution and activity of alkaline phosphatase (E.C. 3.1.3.1), acid phosphatase (E.C. 3.1.3.2), catalase (E.C. 1.11.1.6), xanthine oxidase (E.C. 1.2.3.2), aldolase (E.C. 4.1.2.7 and 4.1.2.13), ribonuclease (E.C. 2.7.7.16) and carbonic anhydrase (E.C. 4.2.1.1) were studied in the major components of bovine milk. Fractionation was accomplished by centrifugation of milk, skim-milk and buttermilk, and ammonium sulphate precipitation of skim-milk serum. The range of activities found for the enzymes studied are tabulated together with the activities of some of the enzymes in mastitic milk, and the significance of the results obtained is discussed. No carbonic anhydrase activity was detected in any of the samples tested. The other enzymes studied were found to have a greater proportion of their total activity located in the skim-milk fraction. However, all of these enzymes except ribonuclease had a higher specific activity in the fat fraction.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 2 , June 1970 , pp. 279 - 288
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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

Aurand, L. W., Chu, T. M., Singleton, J. A. & Shen, R. (1967). J. Dairy Sci. 50, 465.CrossRefGoogle Scholar
Ball, E. G. (1939). J. biol. Cham. 128, 51.CrossRefGoogle Scholar
Bingham, E. W. & Zittle, C. A. (1963). Archs Biochem. Biophys. 101, 471.CrossRefGoogle Scholar
Bingham, E. W. & Zittle, C. A. (1964). Archs Biochem. Biophys. 106, 235.CrossRefGoogle Scholar
Brunner, J. R. (1965). J. Dairy Sci. 47, 907.Google Scholar
Copius Peereboom, J. W. (1968). Ned. Melk- en Zuiveltijdschr. 22, 137.Google Scholar
Corbin, E. A. & Whittier, E. O. (1965). In Fundamentals of Dairy Chemistry, p. 25. (Eds. Webb, B. H. and Johnson, A. H.). Westport, Conn.: Avi Publishing Co.Google Scholar
Dolby, R. M. (1954), J. Dairy Res. 21, 78.CrossRefGoogle Scholar
Garen, A. & Levinthal, C. (1960). Biochim. biophys. Acta 38, 470.CrossRefGoogle Scholar
George, P. (1952). Adv. Catalysis 4, 367.Google Scholar
Gornall, A. G., Bardawill, C. J. & David, M. M. (1949). J. biol. Chem. 177, 751.CrossRefGoogle Scholar
Herskovits, J. J., Masters, C. J., Wassarman, P. M. & Kaplan, N. O. (1967). Biochem. biophys. Res. Commun. 26, 24.CrossRefGoogle Scholar
Hwang, Q., Ramachandran, K. S. & Whitney, R. McL. (1967). J. Dairy Sci. 50, 172.CrossRefGoogle Scholar
Kalnitsky, G., Hummel, J. P. & Dierks, C. (1959). J. biol. Chem. 234, 1512.CrossRefGoogle Scholar
McKenzie, H. A. (1967). Adv. Protein Chem. 22, 55.CrossRefGoogle Scholar
McMeekin, T. L. & Polis, B. D. (1949). Adv. Protein Chem. 5, 201.CrossRefGoogle Scholar
Malveaux, F. J. & San Clemente, C. L. (1969). J. Bact. 97, 1209.CrossRefGoogle Scholar
Morton, R. K. (1953 a). Biochem. J. 55, 786.CrossRefGoogle Scholar
Morton, R. K. (1953 b). Biochem. J. 55, 231.Google Scholar
Morton, R. K. (1956). J. Dairy Sci. 39, 528.Google Scholar
Pereira, R. R., Kristoffersen, T. & Harper, W. J. (1962). J. Dairy Sci. 45, 645.Google Scholar
Polis, B. D. & Shmukler, H. W. (1950). J. Dairy Sci. 33, 619.CrossRefGoogle Scholar
Shahani, K. M. (1966). J. Dairy Sci. 47, 907.CrossRefGoogle Scholar
Sibley, J. A. & Lehninger, A. L. (1949). J. biol. Chem. 177, 859.CrossRefGoogle Scholar
Wilbur, K. M. & Anderson, N. G. (1948). J. biol. Chem. 176, 147.CrossRefGoogle Scholar
Zittle, C. A. (1964). J. Dairy Sci. 47, 202.CrossRefGoogle Scholar
Zittle, C. A., Dellamonica, E. S., Custer, J. H. & Rudd, R. K. (1956). J. Dairy Sci. 39, 528.CrossRefGoogle Scholar