Plant Extracts. Mushroom Extracts. Animal Extracts. Fruit Powder. Vegetable Powder. Vegetarian Protein. Other Products. Home Pepsin Pepsin. Pepsin is one of the principal protein degrading or proteolytic enzymes in the digestive system. During the process of digestion, Pepsin acts on the complex dietary protein and breaks up into peptides and amino acids which can be readily absorbed by the intestinal lining.
It helps in digestive disturbance in general and as a result of impaired production of gastric juice. It acts as an adjunct in the treatment of anemic conditions, especially during slimming diet when protein intake increases.
It is used as research tool in protein analysis and as digestive syrup in heart burn, acid indigestion and sour stomach. It is also used in tablets for increasing appetite and in the preparation of cheese and other protein-containing foods. Catalog NATE Other important digestive proteases are the pancreatic enzymes trypsin and chymotrypsin.
Pepsin denatures if the pH is more than 5. Pepsin is potently inhibited by the peptide inhibitor pepstatin. Autolysis may also be prevented by storage of pepsins at pH 11 or by using pepsins modified by e.
When the pH is adjusted back to pH 6 activity returns. Category : EC 3. Read what you need to know about our industry portal bionity. My watch list my. My watch list My saved searches My saved topics My newsletter Register free of charge. Keep logged in. Cookies deactivated. To use all functions of this page, please activate cookies in your browser. Login Register. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin remains in the larynx following a gastric reflux event.
Pepsin is one of the primary causes of mucosal damage during laryngopharyngeal reflux. Pepsin may also cause mucosal damage during weakly acidic or non-acid gastric reflux. Weak or non-acid reflux is correlated with reflux symptoms and mucosal injury. Upon cellular uptake, pepsin is stored in intracellular vesicles of low pH at which its enzymatic activity would be restored.
Pepsin is retained within the cell for up to 24 hours. Pepsin in airway specimens is considered to be a sensitive and specific marker for laryngopharyngeal reflux.
A rapid non-invasive pepsin diagnostic called Peptest is now available which determines the presence of pepsin in saliva samples. Pepsin may be inhibited by high pH see "Activity" and "Stability", above or by inhibitor compounds. The statyl residue of pepstatin is thought to be responsible for pepstatin inhibition of pepsin; statine is a potential analog of the transition state for catalysis by pepsin and other acid proteases. Pepstatin does not covalently bind pepsin and inhibition of pepsin by pepstatin is therefore reversible.
Pepsin also undergoes feedback inhibition; a product of protein digestion slows down the reaction by inhibiting pepsin. Commercial pepsin is extracted from the glandular layer of hog stomachs.
It is a component of rennet used to curdle milk during the manufacture of cheese. Pepsin is used for a variety of applications in food manufacturing: to modify and provide whipping qualities to soy protein and gelatin, [34] to modify vegetable proteins for use in nondairy snack items, to make precooked cereals into instant hot cereals, [35] and to prepare animal and vegetable protein hydrolysates for use in flavoring foods and beverages.
It is used in the leather industry to remove hair and residual tissue from hides and in the recovery of silver from discarded photographic films by digesting the gelatin layer that holds the silver. Edward E. Pepsin is commonly used in the preparation of F ab' 2 fragments from antibodies. In some assays, it is preferable to use only the antigen-binding Fab portion of the antibody. For these applications, antibodies may be enzymatically digested to produce either an Fab or an F ab' 2 fragment of the antibody.
To produce an F ab' 2 fragment, IgG is digested with pepsin, which cleaves the heavy chains near the hinge region. The light chains remain intact and attached to the heavy chain. The Fc fragment is digested into small peptides. Fab fragments are generated by cleavage of IgG with papain instead of pepsin. Papain cleaves IgG above the hinge region containing the disulfide bonds that join the heavy chains, but below the site of the disulfide bond between the light chain and heavy chain.
This generates two separate monovalent containing a single antibody binding site Fab fragments and an intact Fc fragment. The fragments can be purified by gel filtration, ion exchange, or affinity chromatography. Fab and F ab' 2 antibody fragments are used in assay systems where the presence of the Fc region may cause problems.
The large intestine is mainly responsible for storing waste, reclaiming water, maintaining the water balance, and absorbing some vitamins, such as vitamin K. The large intestine is divided into the cecum, colon, rectum, and anal canal. The gastrointestinal system breaks down particles of ingested food into molecular forms by enzymes through digestion and then transferred to the internal environment by absorption. Find out more about these processes carried out by the gastrointestinal system through this tutorial Read More.
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