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The effect of the modification of arginine side chains in casein on the coagulation of rennin-altered casein

Published online by Cambridge University Press:  01 June 2009

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

The modification of arginine residues in casein by treatment with glyoxal at pH 8·6 resulted in an inhibition of the coagulation of rennin-treated casein. The effective residues are on the κ-casein fraction and inhibition of coagulation was complete when about 1·5 residues of arginine/mole of κ-casein had been altered. It is suggested that the arginine forms part of a positively charged region that also includes lysine and histidine residues, and that this region is important in the coagulation of the casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 2 , June 1970 , pp. 187 - 192
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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References

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