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The specificity for κ-casein as the stabilizer of αs-casein and β-casein II. Replacement of κ-casein by detergents and water-soluble polymers

Published online by Cambridge University Press:  01 June 2009

Margaret L. Green
Margaret L. Green
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9AT
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Summary

The cationic detergent cetyltrimethylammonium bromide (CTAB), the anionic detergents sodium lauryl sulphate and sodium deoxycholate, and the nonionic detergents Tween 20, Tween 80 and Brij 35, and lecithin, starch, glycogen, chondroitin sulphate and polyethylene glycol, were tested for their ability to replace κ-casein in stabilizing αs- and β-caseins against precipitation by Ca2+. Of the materials tested, CTAB and Tween 20 stabilized both caseins and Brij 35 stabilized only αs-casein. Analytical ultracentrifugation of mixtures of CTAB with each casein and of Brij 35 with αs-casein indicated that both detergents acted by disrupting the casein aggregates and complexing with the monomers. Addition of CaCl2 did not aggregate the Brij 35–αs-casein complex. It is concluded that the basis of the stabilization phenomenon involves specific interactions between κ-casein and αs-casein or β-casein at mainly hydrophobic sites.

Type
Original Articles
Information
Journal of Dairy Research , Volume 38 , Issue 1 , February 1971 , pp. 25 - 32
Copyright
Copyright © Proprietors of Journal of Dairy Research 1971

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References

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