Hysteresis in sorption
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A series of sorptions and desorptions of water vapour at 30° C., on gelatin, casein, egg albumin, denatured casein, denatured egg albumin have been conducted and in these systems either there is no hysteresis loop at all or the loop initially exhibited disappears on successive sorptions and desorptions.
These results indicate that the swelling of the adsorbent on imbibing the solvating liquid is responsible for the disappearance of the hysteresis effect.
Experiments on the sorption of ethyl alcohol at saturation pressure on the above proteins at 30°C. show that the nonsolvating liquid is either not adsorbed at all or taken up to a very small extent.
With casein and egg albumin, the sorptive capacities for water are lower in the denatured forms of the proteins. These results indicate a decrease in hydrophilic character of the proteins on denaturation.