Abstract
Plants are rich in protease inhibitors (PI) and trypsin inhibitors are the most common. Therefore, it is of interest to screen PI from plant sources. We report the screening, purification and characterization of PI from Capsicum frutescenes. The partially purified PI showed bands corresponding to 21 KDa and was further confirmed using reverse zymography. The enzyme was stable at temperatures below 60°C and a wide range of pH with 65 folds purification. The effect of magnesium ions oxidizing and reducing agents on PI is reported. The large-scale isolation and purification of PI from Capsicum frutescenes is of commercial interest.
Highlights
Protease inhibitors (PIs) are peptides or proteins proficient of impeding the catalytic activity of proteolytic enzymes
Caseinolytic plate assay: Out of 18 plants screened for the presence of PI, 11 of them showed trypsin inhibitory activity in the primary screening over casein agar plates (Table 1)
Crude samples prepared from the leaves of Capsicum frutescens (CF) were partially purified by ammonium sulphate precipitation and evaluated for their inhibitory activity
Summary
Protease inhibitors (PIs) are peptides or proteins proficient of impeding the catalytic activity of proteolytic enzymes. They can be found in all kingdoms of cellular life including viral genomes, exhibiting its wide distribution in nature [1, 2]. The importance of proteolysis in biological processes is reflected by the percentage of genes encoding for proteases and protease inhibitors, accounting for about 2-4% of the genome [3] These proteases and its inhibitors are known since 20th century and their identification has become more effective because of protease degradomics [4], and association with proteomic tools and enzymatic assays can result in efficient characterization of a number of novel protease inhibitors. Deficiencies or alterations in the regulation of these enzymes determine distinct pathological conditions like cancer, arthritis, neurodegenerative and cardiovascular diseases [9, 10]
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