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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]
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]
An earlier study [13] had highlighted the similarity in specificity of caricain, chymopapain and papain. All seven bonds of the oxidized B chain of insulin that were hydrolyzed by caricain were also cleaved by papain, and six were hydrolyzed by chymopapain. Caricain can be assayed with Bz-ArgkNHPhNO2, kcat/Km being 187 M21 s21 at pH 6.8 and 40˚C.
In the MEROPS protease enzyme classification system, papain-like proteases form Clan CA. [2] Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile. [1] The human genome encodes eleven cysteine cathepsins which have a broad range of physiological functions. [3]
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 enzyme papain can be used to cleave an immunoglobulin monomer into two Fab fragments and an Fc fragment. Conversely, the enzyme pepsin cleaves below the hinge region, so the result instead is a F(ab') 2 fragment and a pFc' fragment. Recently another enzyme for generation of F(ab') 2 has been commercially available.
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]
Optimal temperature ranges of papain and ficin are elevated relative to zingibain, whereas bromelain operates at a slightly lower range. [7] Maximum proteolytic activity of zingibain occurs at pH of 6.0, although the enzyme is still active in pH ranges from 4.5 to 6.0 (optimal pH for meat marinades). [7]