9001-73-4

Usage

Uses

Used in Food Industry:
Papain is used as a meat tenderizer for improving the texture and tenderness of meats. It is also used for clearing beverages, enhancing their clarity and taste.
Used in Leather Industry:
Papain is used as a bating agent for softening and loosening the fibers in skins, making them more pliable and easier to process.
Used in Cosmetics:
Papain is used as a gentle exfoliant in face masks and peeling lotions due to its ability to dissolve keratin. It is considered a non-comedogenic raw material and is less irritating to the skin compared to bromelin, a similar enzyme found in pineapples.
Used in Pharmaceutical Industry:
Papain is used in a patented process where it is injected into the circulatory system of live animals. The enzyme is activated by the heat of cooking to break down proteins, thus tenderizing the beef. However, it is important to note that papain can cause allergic manifestations, and proper protection is required to prevent inhalation of dust and contact with skin or eyes.

Originator

Papain,Green Cross ,Japan,1969

Manufacturing Process

Crude papain, obtained as the dried exudate of the fruit and leaves of Carica papaya L., Caricaceae, is usually found to have been contaminated during collection, drying, or storage by insects, rodent hair and excreta, botanical plant parts, sand, etc. and may thereby become further contaminated by harmful bacteria and enteric organisms. Heretofore papain has been purified by dispersing the crude enzymes in water, filtering and spray-drying. In this procedure, however, the soluble contaminants are retained in the dried product. It has also been known to purify papain by dispersing it in water and adding acetone to reprecipitate the enzymes leaving many of the acetone-soluble and water-soluble impurities in the supernatant liquid. The material thus purified possesses a very disagreeable sulfidelike taste probably due to the reaction between the acetone and reactive sulfhydryl groups present in the papaya latex.It has now been found that an enzyme mixture of high purity which contains none of the objectionable sulfidelike taste can be obtained by dispersing the crude enzymes in water, adding a quantity of a water-miscible lower-alkanol to the incipient precipitation point of the proteolytic enzymes thereby retaining the maximum proteolytic activity (i.e., the maximum amount of the proteolytic enzymes) in the solvent phase while precipitating the major portion of the lower-alkanol insoluble contaminants, removing the loweralkanol insoluble contaminants and precipitated inert materials, for example, by filtration or centrifugation, and then adding an additional quantity of the water-miscible lower-alkanol sufficient to precipitate the proteolytic enzymes. The following is a specific example of the conduct of the present process. 100 g of crude papain were stirred with 120 ml of 0.01 M cysteine hydrochloride for one hour during which time the papain was completely dispersed. To the dispersion was added slowly and with vigorous stirring 147 ml of methanol. The mixture, which contained 55% methanol by volume, was stirred for about thirty minutes and centrifuged and the clear supernatant liquid was removed and saved. The precipitate was washed with 50 ml of 55% aqueous methanol, and the mixture was centrifuged again. The precipitate containing the undesirable, insoluble contaminants was discarded, and the clear wash liquid was combined with the main supernatant. To the combined clear supernatant liquid was added slowly and with vigorous stirring 265 ml of methanol to give a mixture containing 75.5% methanol by volume. The enzymes were precipitated as a taffylike gum which was isolated by decantation of the supernatant liquid containing the undesirable, soluble contaminants and traydrying. Alternatively, the precipitated enzymes can be redissolved in pure water and spray-dried

Therapeutic Function

Enzyme, Wound adhesion inhibitor

Biological Activity

papain is a cysteine protease of the peptidase c1 family, which is used in food, pharmaceutical, textile, and cosmetic industries.

Biochem/physiol Actions

Papain is a cysteine protease that cleaves peptide bonds and is known to cleave the Fc portion of antibodies.

Safety Profile

Poison by intraperitoneal route. Human systemic effects by ingestion: changes in structure or function of esophagus. Experimental teratogenic and reproductive effects. An allergen. When heated to decomposition it emits toxic fumes of NOx.

Purification Methods

A suspension of 50g of papain (freshly ground in a mortar) in 200mL of cold water is stirred at 4o for 4hours, then filtered through a Whatman No 1 filter paper. The clear yellow filtrate is cooled in an ice-bath while a rapid stream of H2S is passed through it for 3hours, and the suspension is centrifuged at 2000rpm for 20minutes. Sufficient cold MeOH is added slowly with stirring to the supernatant to give a final MeOH concentration of 70 vol%. The precipitate, collected by centrifugation for 20minutes at 2000rpm, is then dissolved in 200mL of cold water, the solution is saturated with H2S, centrifuged, and the enzyme is again precipitated with MeOH. The process is repeated four times. [Bennett & Niemann J Am Chem Soc 72 1798 1950.] Papain has also been purified by affinity chromatography on a column of GlyGlyTyrArg-agarose [Stewart et al. J Am Chem Soc 109 3480 1986].