Pancreatin contains the pancreatic enzymes trypsin, amylase and lipase. Examples include thrombin, trypsin, and human neutrophil elastase. It inhibits proteases like chymotrypsin, kallikrein, plasmin, thrombin, and trypsin. Specifically, it is an inhibitor of trypsin and papain. The enzyme trypsin can hydrolyze a phosphate-containing peptone. The pancreas secretes the precursors of a number of proteases such as trypsin and chymotrypsin. DD-transpeptidase is mechanistically similar to the proteolytic reactions of the trypsin protein family. Native enteropeptidase is resistant to soybean trypsin inhibitor. Three common endopeptidases that come from the pancreas are pepsin, trypsin, and chymotrypsin. The lima bean can contain anti-nutrients like phytic acids, saponin, oxalate, tannin, and trypsin inhibitors. It is activated into its active form by another enzyme called trypsin. Any trypsin prematurely formed from the inactive trypsinogen is then bound by the inhibitor. Lentils also have antinutrient factors, such as trypsin inhibitors and a relatively high phytate content. The most prominent application of trypsin inhibitor is livestock feed. The enzymes trypsin and chymotrypsin were first purified in the 1930s.