Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands. The product is a mix of enzymes, formed by trypsin and chymotrypsin, that proteolytically cleave peptide bonds and are involved in food digestion.
Pancrelipase protease acts on the peptide bonds within the proteins. The two constituents of the pancrelipase protease, trypsin, and chymotrypsin, are grouped under the family of serine proteases. Trypsin acts on lysine and arginine residues while chymotrypsin acts in hydrophobic residues such as tryptophan, tyrosine and phenylalanine. Both constituents present a catalytic site in the S1 binding pocket formed by a triad of serine, histidine and aspartate.
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