Trypsin Powder CAS 9002-07-7

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Trypsin powder is a type of protease, EC 3.4.4.4, Molecular formula C35H47N7O10, CAS 9002-07-7, It is a serine protease extracted from the pancreas of cows, sheep, and pigs. In vertebrates, it functions as a digestive enzyme. In the pancreas, the precursor of trypsin, trypsinogen, is synthesized and secreted as a component of pancreatic juice. It is restricted by enterokinase or trypsin to break down into activated trypsin, which is an endopeptidase that can cleave the carboxyl side of lysine and arginine residues in polypeptide chains. It not only functions as a digestive enzyme, but also limits the decomposition of precursors of other enzymes such as chymotrypsin, carboxypeptidase, and phosphatidylcholine, thereby activating them. It is the most specific protease and an indispensable tool in determining the amino acid arrangement of proteins.
A type of protease, which is a serine protease extracted from the pancreas of cows, sheep, and pigs, and functions as a digestive enzyme in vertebrates. The precursor of trypsin, trypsinogen, is synthesized and secreted as pancreatic juice components in the pancreas, and is broken down into active trypsin under the restriction of enterokinase or trypsin. It is an endopeptidase that can cleave the carboxyl side of lysine and arginine residues in polypeptide chains. It not only functions as a digestive enzyme, but also restricts the decomposition of precursors such as chymotrypsin, carboxypeptidase, phospholipase, etc. It is the most specific protease and an indispensable tool for determining protein amino acid arrangement.

Trypsin powder is a freeze-dried preparation obtained by extracting and purifying crystals from the pancreas of cows, pigs, and sheep. Easy to dissolve in water, insoluble in organic solvents such as chloroform, ethanol, and ether. At pH 1.8, short-term boiling almost does not inactivate; Heating in alkaline solution causes denaturation and precipitation, while Ca2+has protective and activating effects. The isoelectric point of trypsin is pH 10.1.

 

Bovine trypsin originally consisted of 229 amino acids, containing 6 pairs of disulfide bonds, and its amino acid sequence and crystal structure have been elucidated. Under the self catalysis of enterokinase activity, the peptide bond between the N-terminal lysine and isoleucine residues of zymogen is hydrolyzed, releasing the valin-tiantiantiantian-lysin 6-peptide and generating active trypsin. The bovine trypsin has 223 amino acid residues and a molecular weight of 23800. The serine residue in the active site is an essential serine protease.

 

The chemical structure of pig trypsin is very similar to that of bovine trypsin. In the sequence of amino acid residues, only 41 amino acid residues are different, but the molecular configuration is significantly different. The settlement coefficient S20W is 2.77S, pI=10.8, The thermal stability is more stable than bovine trypsin, and the protective effect of Ca2+on the enzyme is not as significant as that of cattle and sheep. There is no central site for chelating Ca2+. There are 6 pairs of disulfide bonds, and breaking 1-2 bonds does not damage the complete structure of the enzyme molecule and protects its activity. The enzyme activity is equivalent to 72% of cattle and 61% of sheep, respectively.

Sheep trypsin is similar to that of cattle and pigs, but its activity is slightly higher than that of cattle and pigs.
The specific action of trypsin involves peptide bonds composed of alkaline amino acids arginine and lysine carboxyl groups. Enzymes themselves are easily autolytic, converting from β - trypsin to α - trypsin, which is further degraded into trypsin like enzymes, and even fragments. Their activity gradually decreases and is lost.

 

In addition to being present in vertebrates, it also exists in a wide range of organisms such as silkworms, sea chariots, barnacles, and actinomycetes. In addition, proteases such as thrombin, fibrinolytic enzyme, and vasopressin, which are related to blood coagulation and inflammation in higher animals, are closely related to trypsin in terms of chemical structure and specificity. It can be considered that these enzymes have evolved from a common ancestor enzyme. Trypsin and elastase also have a close relationship in terms of structure and catalytic mechanism, but their specificity is completely different.

 

Trypsin is a proteolytic enzyme extracted from the pancreas of cows, sheep, or pigs. According to Chinese drug standards, the potency of each 1mg should not be less than 2500 units calculated based on the dry product. A peptide endonuclease extracted from the pancreas of cows, sheep, and pigs, which breaks only the peptide bonds formed by the carboxyl groups of lysine or arginine. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform, and ether. Molecular weight 24000, pI 10.5, The optimal pH value is around 7.8-8.5. PH>9.0 irreversible inactivation. Ca2+has a stabilizing effect on enzyme activity; Heavy metal ions, organic phosphorus compounds DFP, Natural trypsin inhibitors strongly inhibit its activity. Clinically used for anti-inflammatory and anti-inflammatory purposes, and industrially used in leather manufacturing, raw silk processing, food processing, etc.

Preparation method of trypsin powder:

Physical and chemical properties of trypsin powder:

Trypsin is a freeze-dried preparation made from the crystals extracted from the pancreas of cattle, pigs and sheep and purified. Easily soluble in water, insoluble in chloroform, ethanol, ether and other organic solvents. At pH 1.8, boiling for a short time hardly inactivates; When heated in alkaline solution, denaturation precipitates, Ca2+has protection and activation effect, and the isoelectric point of trypsin is pH10.1.
Bovine trypsin is composed of 229 amino acids and contains 6 pairs of disulfide bonds. Its amino acid sequence and crystal structure have been clarified. Under the active autocatalysis of enterokinase, the peptide bond between the N-terminal lysine and isoleucine residues of the zymogen is hydrolyzed, releasing Val - day - day - day - day - day - lysine 6 peptide, and producing active trypsin. Bovine trypsin has 223 amino acid residues with molecular weight of 23800. The serine residues in the active site are indispensable serine.

The chemical structure of porcine trypsin is very similar to that of bovine trypsin. In the sequence of amino acid residues, only 41 amino acid residues are different, but the molecular configuration is very different. The sedimentation coefficient S20W is 2.77S, pI=10.8, and the thermal stability is more stable than that of bovine trypsin. The protective effect of Ca2+on enzyme is not as obvious as that of cattle and sheep, and there is no central part of chelating Ca2+. There are 6 pairs of disulfide bonds and 1~2 bonds broken, which will not destroy the complete structure of the enzyme molecule and protect the activity of the enzyme. The enzyme activity is equivalent to 72% of cattle and 61% of sheep. Sheep trypsin is similar to that of cattle and pigs, but its activity is slightly higher than that of cattle and pigs.

Trypsin specifically acts on peptide bonds composed of basic amino acids arginine and lysine carboxyl. The enzyme itself is easy to autolyse β- Trypsin is converted to α- Trypsin is further degraded into tryptase, and even fragments, and its activity is also gradually decreased and lost.

In addition to vertebrates, it also exists in a wide range of organisms, such as silkworm, marijuana, crayfish and actinomycetes. In addition, thrombin, fibrinolytic enzyme, vasodilator and other proteases related to blood coagulation and inflammation of higher animals are closely related to trypsin in terms of chemical structure and specificity. It can be considered that these enzymes are differentiated from common ancestor enzymes in the process of evolution. Chymotrypsin and elastase are also closely related in structure and catalytic mechanism, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from the pancreas of cattle, sheep or pigs. The Chinese drug standard stipulates that the potency of each 1mg of dried product shall not be less than 2500 units. An endopeptidase extracted from the pancreas of cattle, sheep and pigs, which only breaks the peptide bond formed by the carboxyl group of lysine or arginine. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerin, chloroform and ether. The molecular weight is 24000, pI 10.5, and the optimum pH value is about 7.8~8.5. Irreversible inactivation at pH>9.0. Ca2+can stabilize enzyme activity; Heavy metal ions, organophosphorus compounds, DFP, and natural trypsin inhibitors strongly inhibit its activity. It is used for anti-inflammatory and detumescence in clinic and for leather manufacturing, raw silk processing and food processing in industry.

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