Hostname: page-component-848d4c4894-4rdrl Total loading time: 0 Render date: 2024-06-28T06:22:00.047Z Has data issue: false hasContentIssue false

A viscometric study of the breakdown of casein in milk by rennin and rennet

Published online by Cambridge University Press:  01 June 2009

G. W. Scott Blair
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading
J. C. Oosthuizen
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading

Summary

In the later stages of the reaction between rennin and casein drastic viscometric methods are undesirable, but in the first stages there is a fall in viscosity which may be satisfactorily measured in an Ostwald viscometer. Using fat-free milk, the viscosity at first falls linearly with time. At low rennet concentrations (Ce) this may be said to constitute a zero-order reaction (constant k0). At higher rennet concentrations and after longer times, the reaction passes to first order (constant k1). After very long times it doubtless becomes more complex.

The values of k0 are proportional, over a considerable range, to the milk concentration (Cm), those of k1 being independent of Cm.

For pure rennin k0 and k1 are proportional to Ce, but for commercial rennets they vary as a power (N) of Ce and the value of N appears to measure the rennin purity. The potentialities of the method for assessing rennet activities are also discussed.

If the reduced viscosity (specific viscosity÷Cm) of fat-free milks is plotted against Cm, good straight lines are obtained which may be extrapolated to zero concentration to give a reliable value of intrinsic viscosity. The intrinsic viscosity falls progressively during the protein breakdown process but the slope of the curves (‘second order term’) remains unchanged.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1961

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

Alais, C., Mocquot, G., Nitschmann, H. & Zahler, P. (1953). Helv. chim. acta, 36, 1955.Google Scholar
Brown, A. J. (1902). J. chem. Soc. 81, 373.CrossRefGoogle Scholar
Brown, H. T. & Glendinning, T. A. (1902). J. chem. Soc. 81, 388.Google Scholar
Garnier, J. (1957 a). Ann. Technol. 3, 245.Google Scholar
Garnier, J. (1957 b). Proc. Int. Symp. Enzyme Chem., p. 524. Tokyo and Kyoto.Google Scholar
Guggenheim, E. A. (1926). Phil. Mag. 2 (7th ser.), 538.CrossRefGoogle Scholar
Guth, E. (1936). Kolloidzschr. 74, 147.Google Scholar
Hatschek, E. & Jane, R. S. (1926). Kolloidzschr. 39, 300.Google Scholar
Irving, G. W., Fruton, J. S. & Bergmann, M. (1941). J. biol. Chem. 188, 231.Google Scholar
Nitschmann, H. & Bohren, H. U. (1955). Helv. chim. acta, 38, 1953.CrossRefGoogle Scholar
Scott Blair, G. W. (1941). Biochem. J. 35, 267.Google Scholar
Scott Blair, G. W. & Burnett, J. (1958 a). J. Dairy Res. 25, 298.Google Scholar
Scott Blair, G. W. & Burnett, J. (1958 b). J. Dairy Res. 25, 457.CrossRefGoogle Scholar
Scott Blair, G. W. & Oosthuizen, J. C. (1960). Brit. J. appl. Phys. 11, 332.Google Scholar
Söhngen, N. L., Wieringa, K. T. & Pasveer, A. (1937). Rec. Trav. Chim. Pays-bas, 56, 280.Google Scholar
Sterling, C. (1958). J. Dairy Res. 25, 307.CrossRefGoogle Scholar