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The role of lysine residues in the coagulation of casein

Published online by Cambridge University Press:  01 June 2009

R. D. Hill  and
Barbara A. Craker
R. D. Hill
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia
Barbara A. Craker
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia
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Summary

Coagulation of rennin-treated casein was inhibited by treatment of the casein with dimethylaminonaphthalene sulphonyl chloride. The effect was caused by substitution on lysine side chains of the κ-casein fraction, and inhibition was complete when 2–3 lysine residues/molecule were blocked. This level of substitution did not affect other properties of the κ-casein, such as the release from it of non-protein nitrogen (NPN) by rennin and its ability to stabilize αs-and β-caseins in the presence of Ca++. The evidence suggests that lysine side chains on κ-casein take part in the coagulation of rennin-treated casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 35 , Issue 1 , February 1968 , pp. 13 - 18
Copyright
Copyright © Proprietors of Journal of Dairy Research 1968

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References

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