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papain
Papain, also known as Carica papaya protease, is a cysteine protease derived from the latex of the papaya fruit. Its molecular weight is approximately 20,700 Da when determined by sedimentation-diffusion methods, and around 23,000 Da based on amino acid composition analysis. As a thiol protease, papain exhibits broad substrate specificity, breaking down a wide range of proteins more effectively than many pancreatic proteases. In addition to its proteolytic activity, papain also possesses lipase activity.
One unit of papain is defined as the amount required to hydrolyze 1 micromole of benzoyl-L-arginine ethyl ester per minute at 25°C and pH 6.2. The enzyme consists of a single polypeptide chain composed of 211 amino acid residues, folded into two distinct domains with a central cleft. It contains only one essential sulfhydryl group, which plays a critical role in its catalytic function. Cysteine, dithiothreitol (DTT), sulfite, and EDTA can act as activators, while heavy metals, sulfhydryl reagents, and hydrogen peroxide serve as inhibitors.
The preparation of papain involves several key steps. First, a crude extract is obtained by mixing dried papaya latex with diatomaceous earth and washed sand, then grinding the mixture with a cysteine solution. The suspension is filtered, and the filtrate is collected. Next, the pH is adjusted to 9 using sodium hydroxide to remove insoluble materials. The supernatant is then subjected to ammonium sulfate precipitation at 40% saturation, followed by salt precipitation using sodium chloride.
Afterward, the precipitate is dissolved in a cysteine buffer and allowed to crystallize. Crystals are collected via centrifugation and further recrystallized using a sodium hydride solution or methanol-based techniques to enhance purity and specific activity. The final product is stable at 4°C and retains about 80% of its activity after six months of storage. This detailed process ensures high-quality papain suitable for various industrial and biochemical applications.