An Invariant Casein Substrate for Rennet Standardization, derivable from Diverse Sources of Cows' Milk

Abstract

WHEN rennin or commercial rennets (impure rennins) cause milk to coagulate, it is well known that the primary enzyme action consists in decomposing a part only of the casein, known as ϰ-casein1. Later, either through the activity of the products of decomposition or through loss of protective action, the casein aggregates and finally a gel (curd) is formed.

Access options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Waugh, D. F., and Hippel, P. H. von, J. Amer. Chem. Soc., 78, 4576 (1956).

  2. 2

    Scott Blair, G. W., and Oosthuizen, J. C., J. Dairy Res., 28 (2), 165 (1961).

  3. 3

    Guggenheim, E. A., Phil. Mag. (7th Ser.), 2, 538 (1926).

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Cite this article

BLAIR, G., OOSTHUIZEN, J. An Invariant Casein Substrate for Rennet Standardization, derivable from Diverse Sources of Cows' Milk. Nature 191, 697–698 (1961). https://doi.org/10.1038/191697a0

Download citation

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.