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The effect of the chemical structure of additives on the coagulation of casein micelle suspensions by rennet

Published online by Cambridge University Press:  01 June 2009

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

Casein micelles in milk-salts solution adsorbed charged detergents and highly-charged polypeptides strongly, neutral detergents less strongly and low molecular-weight amines weakly. A tetra-amine was adsorbed more strongly than a tri-amine. The extent of adsorption of proteins tended to rise as the molecular weight increased. Glycerol and lactate were adsorbed to a limited extent but dextran and α-ketoglutarate were not adsorbed at all. Proline was partly adsorbed, indicating that hydrophobic binding sites were available, and caused some disruption of the casein micelles. Additives were bound to approximately the same extent by casein micelles and rennet coagula. The proportions adsorbed were constant over at least 10-fold ranges of concentration. Additives which increased the rennet clotting time (RCT) acted by binding Ca2+. Most additives decreased the RCT, the extent increasing with the amount adsorbed and the positive charge on the additive. The greatest reduction in RCT was observed with those additives which had positively-charged and hydrophobic moieties and bound most strongly to casein micelles. Of the additives tested, only sodium dodecyl sulphate affected the enzymic action of rennet. The reduction in RCT may have resulted from the neutralization of the negative charge of the micelles or enhancement of their hydrophobicity, favouring hydrophobic interactions between the particles.

Type
Original Articles
Information
Journal of Dairy Research , Volume 47 , Issue 3 , October 1980 , pp. 359 - 369
Copyright
Copyright © Proprietors of Journal of Dairy Research 1980

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