PROTEOLYTIC AND PEPTIDOLYTIC ACTIVITIES IN COMMERCIAL PANCREATIC PROTEASE PREPARATIONS AND THEIR RELATIONSHIP TO SOME WHEY-PROTEIN HYDROLYSATE CHARACTERISTICS

Endoproteinase and exopeptidase activities in the commercially availab le pancreatic protease preparations Corolase PP, PTN 3.0S, pancreatin, PEM 2500S, PEM 2700S, and PEM 800S were quantified using synthetic pe ptide substrates. These preparations were generally found to be low in aminopeptidase and dipeptidase activity. Trypsin and chymotrypsin, al beit in different ratios, were present in all pancreatic preparations. Elastase was present only in Corolase PP and pancreatin. The ability of these protease preparations to hydrolyze the insoluble heat denatur ted whey protein, lactalbumin, was compared and contrasted with that o f crystalline trypsin, chymotrypsin, and elastase in addition to a com mercial exopeptidase preparation, Debitrase DBP.20. When the source, n umber, or ratio of endoprotease activity changes, there are distinctiv e differences in products produced with respect to percentage degrees of hydrolysis, gel permeation profile, solubility, and free amino acid s present in the hydrolysate.