Trypsin: Background Serine proteases represent over

Background Serine proteases represent over 1% of all proteins in humans. This family of proteins is found on cell surfaces, subcellular organelles like lysosomes or mitochondria, within the nucleus and the protoplasm. Main body of the abstract Among them, trypsin , chymotrypsin and elastase have aroused great interest because of their numerous functions in pathophysiological processes. Altered expression of these enzymes in experimental animal models and humans has been related to various ... Trypsin is a digestive enzyme produced in the pancreas that plays a crucial role in breaking down proteins into smaller peptides in the small intestine. It is synthesized as an inactive precursor called trypsinogen, which is activated in the small intestine by the enzyme enteropeptidase. This activation process connects trypsin to the larger framework of protein digestion and the overall function of digestive systems. Function Trypsin or serine protease 1 is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was ... Trypsin is a serine protease enzyme that breaks down proteins into peptides in the digestive system. It is also involved in various biological processes, such as cancer, immune defense and food technology. Learn about its structure, function, sources and side effects.