Papain from papaya latex

Papain, a cysteine protease, consists of a single polypeptide chain with three disulfide bridges and a sulfhydryl group.

Papain from papaya latex has been used to digest:

• Muller glial cells
• cartilage explants
• GAG and DNA content of the tissue constructs
• decellularized tissue samples.

Papain is used in dissecting solutions. It is used to produce Fab fragments of antibodies. It is used for cell dissociation since it has been shown to be more effective and less damaging with certain tissues. Papain has been used to isolate morphologically intact cortical neurons from postnatal rats. Limited papain digestion is used for structural studies of enzymes and other proteins. In addition, papain is used in red cell serology to modify the red cell surface to enhance or destroy the reactivity of many red cell antigens. Papain is useful for platelet serology studies. Papain has also been used in the enzymatic synthesis of amino acids, peptides, and other molecules.

Used to produce Fab fragments of antibodies. Also used for cell dissociation since it has been shown to be more effective and less damaging with certain tissues.

Papain has broad specificity, in cleaving peptide bonds of basic amino acids, leucinehydrolyzes esters and amides. Papain digests many protein substrates extensively than pancreatic proteases. Papain is commonly used in cell isolation procedures since it is more efficient and less harmful compared to other proteases. Papain significantly increases the yield of viable smooth muscle cells without affecting the cell′s sensitivity to stimulants. It catalyzes several reactions, like hydrolysis, transferase action, specificity and acyl-enzyme intermediate.

Papain papaya latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.
. The pH optimum is 6.0-7.0
. Papain hydrolyzes esters and amides. Papain consists of a single polypeptide chain with three disulfide bridges and a sulfhydryl group necessary for activity of the enzyme.

A cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.
pH optimum 6.0-7.0
Also hydrolyzes esters and amides.

One unit will hydrolyze 1.0 μmole of N-α-benzoyl-L-arginine ethyl ester (BAEE) per minute at pH 6.2 at 25 °C.

Suspension in 0.05 M sodium acetate, pH 4.5, containing 0.01% thymol

View more information on papain at www.sigma-aldrich.com/enzymeexplorer.