Response of Rat Pancreatic Proteases to Dietary Proteins, Their Hydrolysates and Soybean Trypsin Inhibitor

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Abstract
The present study was designed to determine whether the adaptation of pancreatic trypsin and chymotrypsin activities to dietary protein level can be attributed to the presence in the diet of the specific peptide bonds that are substrates for these enzymes. In addition, the effect of feeding soybean trypsin inhibitor (SBTI) was tested since this compound is known to stimulate synthesis of pancreatic proteases. For 3 weeks, rats were fed a diet containing 10, 20 or 30% protein as lactalbumin (control); lactalbumin predigested by trypsin, chymotrypsin or pancreatin; a mixture of amino acids; or lactalbumin supplemented with SBTI. At the end of the experiment, the activities of trypsin, chymotrypsin and amylase were determined in the rats' pancreatic homogenates. Trypsin and chymotrypsin activities at each protein level were exactly the same whether predigested lactalbumin or lactalbumin was fed. The 20 and 30% amino acid mixtures, however, produced a decrease in activities of both proteases. SBTI doubled the activities of both proteases at all three levels of protein. Amylase activity was maximal at 20% level of protein. It is concluded that adaptation of pancreatic proteases to dietary protein level is induced by small peptides that are digestion products of dietary protein. Induction of pancreatic trypsin or chymotrypsin therefore does not require the presence of substrate for these enzymes in the intestine. Dietary SBTI produced a considerable increase in pancreatic proteases compared to that produced by proteins or peptides. It is suggested that the increases in pancreatic proteases caused either by protein-rich diets or SBTI are mediated by two distinct mechanisms.

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