Abstract
In a previous paper, it has been reported that the hydrolysis rate of casein by alkali protease is much enhanced by the presence of oxidizing agents. This synergetic effect was most enhanced when casein contacted with oxidizing agents before contacting with the enzyme. In the present paper, we report a gel permeation chromatography study on the effect for three other proteins, bovine serum albumin (BSA), ovalbumin (OvA) and gelatin.
The results are summarized as follows :
Successive contact of the proteins with sodium percarbonate and the protease in solution resulted in the enhanced protein degradation, by ca 60% for OvA and ca 10% for gelatin respectively. But no effect was observed for BSA.
When OvA or gelatin was brought into contact with the oxidizing agent, fragments with 104-103 dalton for the former or those with slightly lower molecular weights than the native one for the latter were yielded. However BSA gave no such products at all. It was inferred that the synergetic effect was caused by the faster hydrolysis rates of the degraded fragments by protease than those of the intact substrate proteins.
