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Chymopapain (EC 3.4.22.6, chymopapain A, chymopapain B, chymopapain S, brand name Chymodiactin) is a proteolytic enzyme isolated from the latex of papaya (Carica papaya).It is a cysteine protease which belongs to the papain-like protease (PLCP) group. [1]
The enzyme is deacylated by a water molecule and releases the carboxy terminal portion of the peptide. In immunology, papain is known to cleave the Fc (crystallisable) portion of immunoglobulins (antibodies) from the Fab (antigen-binding) portion. Papain is a relatively heat-resistant enzyme, with an optimal temperature range of 60 to 70 °C. [9]
Papain is a protease obtained from the latex of the fruit of the papaya tree. It has been used (without regulation) for wound debridement for many years, but in the US in 2008 it was brought under regulation by the U.S. Food and Drug Administration and removed from sale for this purpose, following reports of adverse effects. On the other hand ...
[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...
The first description of this enzyme was provided by Schack, [1] who named it papaya peptidase A. The same enzyme has since been given a number of different names, including papaya peptidase II, [4] papaya proteinase III [5] and papaya proteinase. [7] The name caricain was recommended by NC-IUBMB in 1992.
Actinidain (EC 3.4.22.14, actinidin, Actinidia anionic protease, proteinase A2 of Actinidia chinensis) is a type of cysteine protease enzyme found in fruits including kiwifruit (genus Actinidia), pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases. [1] [2] [3] [4]
Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Carica papaya. [1] Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe.
The papain enzyme present in the milky latex of immature fruits and leaves is often used in the culinary industry as a meat tenderizer since it is a digestive enzyme. [7] Traditionally, the mountain papaya fruit is also prepared as an infused drink including passion fruit, apple, and other fruits and is often sold by street vendors. [citation ...
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