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178. A lipase (tributyrinase) of cows' milk. I. Occurrence, method of estimation and relationship to lactation cycle

Published online by Cambridge University Press:  01 June 2009

E. C. V. Mattick  and
H. D. Kay
E. C. V. Mattick
Affiliation:
National Institute for Research in Dairying, University of Reading
H. D. Kay
Affiliation:
National Institute for Research in Dairying, University of Reading
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Extract

An enzyme which hydrolyses tributyrin is present in all samples of fresh cows' milk examined. A method has been developed for the determination of the tributyrinase activity of a given milk or fluid.

In milk the enzyme is present in the aqueous rather than the fatty portion. Its optimal range of activity is in the region pH 8·2–8·7. It is rather more thermolabile than phosphatase.

Its concentration in milk varies considerably from cow to cow, and in individual healthy cows there is a fairly regular variation throughout the lactation cycle. It is highest in concentration in colostrum, then the concentration falls to a minimum at about 10 days, rising later to a figure intermediate between this minimum and the colostral value. It shows no sign of increase towards the end of the lactation period.

Its relationship to the “true lipase” of milk is discussed.

Type
Original Articles
Information
Journal of Dairy Research , Volume 9 , Issue 1 , January 1938 , pp. 58 - 71
Copyright
Copyright © Proprietors of Journal of Dairy Research 1938

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References

REFERENCES

(1) Nair, J. H. (1930). Industr. Engng Chem. 22, 42.CrossRefGoogle Scholar
(2) Rice, F. E. & Markley, A. L. (1922). J. Dairy Sci. 5, 64.CrossRefGoogle Scholar
(3) Richmond, Droop H. (1919). Analyst, 44, 255.Google Scholar
(4) Michaelis, L. (1930). J. biol. Chem. 87, 33.Google Scholar
(5) Sobotka, H. & Glick, D. (1934). J. biol. Chem. 105, 205.CrossRefGoogle Scholar
(6) Willstätter, R. & Memmen, F. (1923). Hoppe-Seyl. Z. 129, 1.CrossRefGoogle Scholar
(7) Hiscox, E. R. & Harrison, J. (1936). Nature, Lord., 138, 32.CrossRefGoogle Scholar
(8) Kay, H. D. & Graham, W. R. (1933). J. Dairy Res. 5, 63.CrossRefGoogle Scholar
(9) Spitzer, G. & Taylor, M. C. (1924). J. Dairy Sci. 7, 234.Google Scholar
(10) Orla-Jensbn, S. (1929). Lait, 9, 622.Google Scholar
(11) Dorner, W. & Widmer, A. (1931) Lait 11, 545.Google Scholar
(12) Sharp, P. F. & De Tomasi, J. A. (1932). Proc. Intern. Soc. Milk Dealers (Lab. Section), 3.Google Scholar