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Its main function is to inhibit a variety of secretory mechanisms. Throughout the lining of the small intestine there are numerous brush border enzymes whose function is to further break down the chyme released from the stomach into absorbable particles. These enzymes are absorbed whilst peristalsis occurs. Some of these enzymes include:
The chyme moves through the jejunum and the ileum, where digestion progresses, and the non-useful portion continues onward into the large intestine. The duodenum is protected by a thick layer of mucus and the neutralizing actions of the sodium bicarbonate and bile. At a pH of 7, the enzymes that were present from the stomach are no longer active.
Chalcone synthase or naringenin-chalcone synthase (CHS) is an enzyme ubiquitous to higher plants and belongs to a family of polyketide synthase enzymes (PKS) known as type III PKS. Type III PKSs are associated with the production of chalcones , a class of organic compounds found mainly in plants as natural defense mechanisms and as synthetic ...
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
Pepsin is expressed as a zymogen called pepsinogen, whose primary structure has an additional 44 amino acids compared to the active enzyme. In the stomach, gastric chief cells release pepsinogen. This zymogen is activated by hydrochloric acid (HCl), which is released from parietal cells in the stomach lining.
The shikimate pathway (shikimic acid pathway) is a seven-step metabolic pathway used by bacteria, archaea, fungi, algae, some protozoans, and plants for the biosynthesis of folates and aromatic amino acids (tryptophan, phenylalanine, and tyrosine). This pathway is not found in mammals.
In vivo, chymotrypsin is a proteolytic enzyme (serine protease) acting in the digestive systems of many organisms. It facilitates the cleavage of peptide bonds by a hydrolysis reaction, which despite being thermodynamically favorable, occurs extremely slowly in the absence of a catalyst. The main substrates of chymotrypsin are peptide bonds in ...
The first plant phytase was found in 1907 from rice bran [3] [4] and in 1908 from an animal (calf's liver and blood). [4] [5] In 1962 began the first attempt at commercializing phytases for animal feed nutrition enhancing purposes when International Minerals & Chemicals (IMC) studied over 2000 microorganisms to find the most suitable ones for phytase production.