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Journal of Dairy Science Vol. 26 No. 11 1043-1056
© 1943 by American Dairy Science Association ®
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Rennin Action in Relation to the Water Binding and Electrokinetic Properties of Calcium and Sodium Caseinate Sols*

C. L. Hankinson{dagger} and L. S. Palmer

Division of Agricultural Biochemistry, University of Minnesota, St. Paul, Minnesota

ABSTRACT

Söhngen, Wieringa and Pasveer (9) proposed a theory supported by viscometry evidence that a certain amount of dehydration of the casein explains the action of rennin as far as the initial stage of the rennin coagulation process is concerned. Richardson and Palmer (7) have shown that rennin decreases the electrokinetic charge on the casein micelles, and since Smoluchowski (8) has shown that a suspension of charged particles is more viscous than one of uncharged particles, the reality of a true dehydration effect is open to question.

Briggs (1) and Hankinson and Briggs (3) investigated the hydration of sodium gum arabic and sodium and calcium caseinate systems by applying the Krasny-Ergen (5) equation for electroviscous effect, which interrelates hydration and the electrokinetic potential. The viscosity relationships in the equation were verified by data on these colloidal systems, but a colloid concentration factor appears to be necessary for proper evaluation of the radius of the micelles.

FOOTNOTES

* Paper No. 2076, Scientific Journal Series, Minnesota Agricultural Experiment Station. The data are taken from the Ph.D. thesis of C. L. Hankinson, University of Minnesota, 1939.

{dagger} Present address: Carnation Company Research Laboratory, Milwaukee, Wisconsin.






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Copyright © 1943 by the American Dairy Science Association ®.