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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]
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]
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]
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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.
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.
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