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.
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References
Waugh, D. F., and Hippel, P. H. von, J. Amer. Chem. Soc., 78, 4576 (1956).
Scott Blair, G. W., and Oosthuizen, J. C., J. Dairy Res., 28 (2), 165 (1961).
Guggenheim, E. A., Phil. Mag. (7th Ser.), 2, 538 (1926).
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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
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DOI: https://doi.org/10.1038/191697a0
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