CHYMOPAPAIN Chemical Properties

storage temp. 

-20°C

Merck 

13,2281

Safety Information

Hazard Codes 

Xn

Risk Statements 

36/37/38-42/43

Safety Statements 

23-26-36/37-45

RTECS 

GC2800000

CHYMOPAPAIN Usage And Synthesis

Originator

Chymodiactin,Smith,US,1982

Uses

Chymopapain from papaya latex has been used in a study to assess the anthelmintic effect of natural plant cysteine proteinases against the gastrointestinal nematode, Heligmosomoides. Chymopapain from papaya latex has also been used in a study to investigate the preparation and identification of the rabbit′s antibody of chymopapain.

Uses

In meat tenderizer.

Manufacturing Process

The undried latex of papaya is mixed with about three times its weight of hundredth normal hydrochloric acid. To this mixture is then added dilute hydrochloric acid (about normal) until a pH of substantially 2 has been
attained. The acidified latex is next allowed to stand over night or longer in a cold place (0°C to 10°C). The material still in solution is then separated out, by any convenient means, such as filtration through paper. From the soluble portion, a small amount of inert protein is precipitated, by half saturation with sodium chloride at about 10°C. The desired enzyme is next precipitated as a nearly pure protein by raising the concentration of salt to full saturation, while the pH is kept at a level of substantially 2, by the addition of normal alkali, if necessary. The precipitate of protein is removed by any suitable means, and may be kept as a thick paste out of contact with the air, and in the cold, The keeping properties at higher temperatures are enhanced by addition of enough alkali to the protein to bring its pH to 4.5-6.0.
This protein may be further purified, if desired, and eventually may be crystallized, by redissolving the paste in saturated sodium chloride solution by adjusting the pH to 4.5-6.0, and reprecipitating the enzyme protein by the gradual addition of acid in the cold, until a pH of approximately 2.0 is obtained; or, the purification may be accomplished by dissolving the protein in acid at a pH of 2, and then precipitating the enzyme, by increasing the concentration of salt.
When the activity and other properties of the several times recrystallized new enzyme protein are compared with those of the uncrystallized precipitate obtained in the first stages of the process, it is found that even in the first stages, the enzyme is present in sufficiently pure form for most purposes

brand name

Chymodiactin (Abbott); Discase (Abbott).

Biochem/physiol Actions

The enzyme cleaves amide linkages at the carboxyl side of arginine, leucine, glutamic acid, and alanine residues; as well as that of arginine esters. The optimum pH varies depending on the kind of substrate. For example, the pH optimum for casein digestion is 7.9, hemoglobin digestion is 4.0 and urea-denatured hemoglobin digestion is 7.0. Molecular mass of the enzyme is found to be 27 KDa.

CHYMOPAPAIN(9001-09-6)Related Product Information

• DISPASE
• N/A
• MG-132
• flavourzyme
• EC 3.4.21.19
• Collagenase
• Bromelain
• CATHEPSIN H
• EC 3.4.21.14
• Proteinase K
• Urinary Trypsin Inhibitor
• DISPASE
• ACHROMOPEPTIDASE
• Trypsin
• MG-115
• trysin-chymotrypsin
• Basic protease
• Papain