Chemical or enzymatic deglycosylation and germination abrogates the inhibitory activity of Cyamopsis tetragonoloba trypsin inhibitor

摘要

Abstract A glycosylated heat stable trypsin chymotrypsin inhibitor was isolated from Cyamopsis tetragonoloba seeds. It is being reported for the first time that deglycosylation of the inhibitor chemically by Trifluoro methane sulfonic acid or enzymatically by salivary amylase or fungal diastase abrogates the inhibitory activity indicating that glycosylation was important for inhibitory activity of the protein. Treatment with salivary amylase decreases the inhibition in in vitro digestion experiment also. Germination of Cyamopsis tetragonoloba seeds results in reduction in inhibitory activity with concomitant increase in amylase activity. It is speculated that increase in amylase during germination decreases the protease inhibitory activity by deglycosylating the inhibitor.