1962 Volume 35 Issue 2 Pages 240-244
The mode of the binding of detergents, SDBS, CPC and DPB, by gelatin in the region of low detergent-gelatin ratios, where solutions are stable without precipitation, was investigated by determining the bound detergents by means of equilibrium dialysis.
Detergents bind with gelatin in accordance with the isotherm r=Kcn, where K and n (>1) are constants which measure an affinity for the binding and an extent of cooperative interaction respectively. The value of K, which is dependent on pH and temperature, decreases with increasing pH for the binding of SDBS and vice versa for CPC. The value of n is characteristic of a given detergent. The value of n for SDBS is significantly greater than that for CPC. Thus the extent of the cooperative stabilization of a bound detergent is higher for SDBS than for CPC.
Both anionic SDBS and cationic CPC combine with gelatin, but cationic DPB scarcely combines with it. Further, it was inferred that a detergent, especially SDBS, binds with gelatin, forming aggregates on it in such a manner as the micelle formation.
The sign of charge of the detergent is of essential importance for the binding of the detergent by gelatin, and the length of the alkyl chain of detergent also has additional effects on the binding. The effect of chain length was examined with cationic detergents.
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