Inhibitor from E. frumentacea seeds was modified on storage as well as by the addition of mercaptoethanol. The trypsin/chymotrypsin inhibitor, totally devoid of antichymotryptic activity, was purified 500 folds with 17% recovery of the antitryptic activity. It was more stable to heat, cooking, changes in pH, and digestion by proteolytic enzymes than the native inhibitor. It formed a complex with trypsin in 1:1 stoichiometric ratio. Both arginyl and lysyl groups were found to be necessary for its action.
|Number of pages||6|
|Publication status||Published - 01-01-1998|
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