Proteinase inhibitors in meal ofAnacardium occidentale seeds

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Abstract
Trypsin and chymotrypsin inhibiting activities were detected in a “crude inhibitor” fraction of a lipid free cashew nut (Anacardium occidentale L.) meal. Both activities were shown to be heat resistant and not affected by pepsin at pH 3.0. Molecular weight distribution of tho trypsin inhibiting activity is similar to the known range of molecular weights for trypsin inhibitors of plant origin. A “crude extract” of the cashew nut meal was shown to contain strong L-leucine-p-nitro-anilide and moderately strong α-N-benzoyl-DL-arginine-p-nitroanilide hydrolyzing activities. This last activity was strongly inhibited by the “crude inhibitor” fraction shown to contain trypsin and chymotrypsin inhibiting activities. The presence of this endogenous inhibitor-endo-peptidase system seems to indicate that the protein proteinase inhibitors of plant origin could be involved in the control of protein mobilization in the seed.

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