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Description
Papain is a widely used plant protease. It is made from the immature fruit of papaya by extracting emulsion, solidification, settling and drying. Papain is pure natural, safe and toxin-free, now widely used in the food processing industry, beer brewing and meat tenderizing industries.
Papain is soluble in water and glycerin, and the solution is colorless, sometimes milky white. Almost insoluble in ethanol, chloroform and other organic solvents. The most suitable PH value is 5.7 (generally 3~9.5), and it also can be used in neutral or acidic condition. The most suitable temperature is 55~60 ° C (generally 10~85 ° C) with strong heat resistance, and it will not be completely deactivated at 90 ° C.
Papain has the characteristics of high enzyme activity, strong thermal stability, safety and hygiene, and has been widely used in food, cosmetics, medicine and health care products, daily chemicals, feed, leather, textile and other industries.
Function:
1. Meat tenderizer, Noodle stabilizer and Biscuit fluffing agent
2. Cleaning the wound and accelerating wound healing
3. Feed supplement
4. Used for soap, detergent, washing powder
5. Hair removal agent and tanning leather
6. Processing wool, silkworm pupa degumming, silk refining
Structure and properties
Papain is a single-chain polypeptide enzyme composed of 212 amino acid residues with a molecular weight of about 23.4 kDa. Its active center contains cysteine residues, which can participate in catalytic reactions through sulfhydryl groups (-SH). Papain is most active in acidic to neutral environments (pH 5-7), but it can still maintain a certain activity in a wider pH range (3-11). In addition, it is sensitive to temperature, with an optimum temperature of 60-70℃, but it is easily inactivated at high temperatures.
Mechanism of action
Papain decomposes large molecular proteins into small molecular peptides or amino acids by hydrolyzing peptide bonds in proteins. Its catalytic action depends on the cysteine residue in the active center, and can specifically recognize the carboxyl terminal peptide bond of hydrophobic amino acids (such as phenylalanine and leucine).
Application:
1. Medicine;
2. Cosmeitcs;
3. Food additive;
4. Feed;
5. Daily Chemical;
6. Leather and textile
Description
Papain is a widely used plant protease. It is made from the immature fruit of papaya by extracting emulsion, solidification, settling and drying. Papain is pure natural, safe and toxin-free, now widely used in the food processing industry, beer brewing and meat tenderizing industries.
Papain is soluble in water and glycerin, and the solution is colorless, sometimes milky white. Almost insoluble in ethanol, chloroform and other organic solvents. The most suitable PH value is 5.7 (generally 3~9.5), and it also can be used in neutral or acidic condition. The most suitable temperature is 55~60 ° C (generally 10~85 ° C) with strong heat resistance, and it will not be completely deactivated at 90 ° C.
Papain has the characteristics of high enzyme activity, strong thermal stability, safety and hygiene, and has been widely used in food, cosmetics, medicine and health care products, daily chemicals, feed, leather, textile and other industries.
Function:
1. Meat tenderizer, Noodle stabilizer and Biscuit fluffing agent
2. Cleaning the wound and accelerating wound healing
3. Feed supplement
4. Used for soap, detergent, washing powder
5. Hair removal agent and tanning leather
6. Processing wool, silkworm pupa degumming, silk refining
Structure and properties
Papain is a single-chain polypeptide enzyme composed of 212 amino acid residues with a molecular weight of about 23.4 kDa. Its active center contains cysteine residues, which can participate in catalytic reactions through sulfhydryl groups (-SH). Papain is most active in acidic to neutral environments (pH 5-7), but it can still maintain a certain activity in a wider pH range (3-11). In addition, it is sensitive to temperature, with an optimum temperature of 60-70℃, but it is easily inactivated at high temperatures.
Mechanism of action
Papain decomposes large molecular proteins into small molecular peptides or amino acids by hydrolyzing peptide bonds in proteins. Its catalytic action depends on the cysteine residue in the active center, and can specifically recognize the carboxyl terminal peptide bond of hydrophobic amino acids (such as phenylalanine and leucine).
Application:
1. Medicine;
2. Cosmeitcs;
3. Food additive;
4. Feed;
5. Daily Chemical;
6. Leather and textile
