Abstract:Determination of chymotrypsin inhibitor activity is very important for the study of proteins in potato tubers, particularly for protein separation and purification. In this study, a method to evaluate the activity of a potato-derived chymotrypsin inhibitor was explored. This method was based on the spectrophotometric determination (275 nm) of the hydrolysis products of casein that were produced by a specific concentration of chymotrypsin, in the presence or absence of the inhibitor. The results showed that the chymotrypsin inhibitor activity of a crude protein solution extracted from potato tubers was 98.31 CUI/mg (82.11 μg/mg). In other words, each milligram of chymotrypsin inhibitor inhibited 82.11 μg chymotrypsin. Theoretically, the chymotrypsin inhibitor content in 100 g potato tubers can inhibit the activity of 147.43 mg chymotrypsin. Thus, this method is suitable to determine the activity of chymotrypsin inhibitors from potatoes and other sources.
