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Bovine milk protease

Published online by Cambridge University Press:  01 June 2009

J. R. Dulley
J. R. Dulley
Affiliation:
Otto Madsen Dairy Research Laboratory, Department of Primary Industries, Harbour Road, Hamilton, Brisbane 4007, Australia
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Summary

Milk protease, the naturally occurring proteolytic enzyme from fresh raw bovine milk, was purified 629-fold. Purification methods are described which included acid precipitation, ion-exchange and gel chromatography and ammonium sulphate fractionation. It was necessary to use a large-scale purification as the amounts of enzyme in milk are very low.

The basic properties of the enzyme were elucidated from experiments on this partially purified fraction. Under the conditions of assay these showed a wide pH optimum from 6·5 to 9·0 and a temperature optimum of 37°C. The protease was fairly heat stable, the stability being pH dependent.

The source of the enzyme appeared to be the mammary gland, where the enzyme was also detected.

Type
Research Article
Information
Journal of Dairy Research , Volume 39 , Issue 1 , February 1972 , pp. 1 - 9
Copyright
Copyright © Proprietors of Journal of Dairy Research 1972

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References

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