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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]
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 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.
Glycyl endopeptidase (EC 3.4.22.25, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, ... This enzyme catalyses the following chemical reaction.
[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 ...