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Dr. Mohammad Qasim
Department of Chemistry
Indiana University – Purdue University Fort Wayne
Proteases are enzymes which hydrolyze peptide bonds of proteins and peptides, and are involved in a variety of important biological functions such as digestion of food, blood clotting, and activation of many proteins and enzymes. A major class of proteases is the serine protease. Uncontrolled protease activity may produce disastrous results. Another class of proteins, called protease inhibitors, are responsible for regulating the activity of proteases. In this presentation I describe the research I have on serine protease inhibitors in peanuts. I extracted the serine protease inhibitors from roasted peanuts and studied the inhibition of two serine proteases namely chymotrypsin and trypsin. I also studied the effect of pepsin digestion on the inhibitory activity of peanut inhibitors. The objective of this research was to investigate whether the peanut inhibitors are digested by the stomach enzyme like other proteins or whether they are stable and remain undigested. My results suggest that the peanut serine protease inhibitors are stable to the digestion by the stomach enzyme and can inhibit the intestinal proteases, chymotrypsin and trypsin. The results of the research are significant in the sense that they suggest that consumption of peanuts can slow intestinal digestion of proteins.
Chemistry | Physical Sciences and Mathematics
Vilar, Lei, "Effect of Pepsin Digestion on the Inhibitory Activity of Serine Protease Inhibitors in Peanuts" (2015). 2015 IPFW Student Research and Creative Endeavor Symposium. 69.