Pepsin

Introduction:

This product is a pepsin extracted from the gastric mucosa of pigs, sheep or cattle. It is a digestive protease secreted by the main cells of the gastric mucosa in the stomach. The precursor of pepsin is called pepsinogen..

 

Principle:

Pepsinogen is secreted by the main cells of the gastric fundus, and is activated to pepsin at pH 1.5 to 5.0, which breaks down proteins into peptides, and some of them are broken down into amino acids such as tyrosine and phenylalanine. Pepsin has certain amino acid sequence specificity when it cuts protein or polypeptide. For example, it tends to cleave peptide bonds with aromatic amino acids (such as phenylalanine, tryptophan, and tyrosine) or leucine at the amino or carboxyl terminus; and if it is third to the amino terminal of a peptide bond When an amino acid is a basic amino acid (such as lysine, arginine, and histidine) or the amino terminal of the peptide bond is arginine, the peptide bond cannot be effectively cleaved. This shear specificity is even more pronounced at pH 1.3: it tends to cleave only the amino terminus.

 

Product features：
1. Temperature range: The effective temperature range of pepsin is 25-70 ° C, and the optimal temperature range is 37-39 ° C;
2. PH value range: Effective pH range is 1.0-5.5, and optimum pH range is 1.5-2.5;

3. Impact of metal ions on enzyme activity: Pepsin is susceptible to metal ions such as copper and iron, which reduces the activity. Mg2 + and Ca2 + have a certain degree of inhibition on enzyme activity.

 

Product properties：
1. Product specifications: The enzyme active solid is a white or light yellow powder with an enzyme activity of 1000u / mg; the solid enzyme fineness (0.4mm standard sieve pass rate): ≧ 80%.

2. Definition of enzyme activity: at 40 ° C, 1 μg of tyrosine produced per minute of casein hydrolysis is defined as a unit of protease activity.

 

Instructions：
1. Food industry: Utilizing the enzymatic reaction of pepsin, it can hydrolyze the large-molecule protein in food into small-molecule peptides or amino acids. It is used for the hydrolysis of fish meal and other proteins (such as soybean protein), and curd in cheese production Action (combined with rennet).
2. Pharmaceutical industry: treatment of indigestion caused by pepsin deficiency or reduced digestive function. Pepsin is a digestive enzyme. It is often used for indigestion due to lack of pepsin after eating proteinaceous food, digestive dysfunction during recovery period after illness, and loss of appetite and chronic atrophic gastritis. In order to play a role, so often used together.

3. Other industries: biochemical research, protein structure analysis, prevention of refrigerated turbidity of beer, etc. The dosage in other industries is determined according to different substrate concentrations and operating conditions. It is recommended to start with low-dose experiments under the guidance of professional technicians.

 

Packaging and storage：
The solid is packed in food packaging bags, 20kg / bag.

Pepsin is recommended to store in a cool and dry place, with a relative humidity of less than 60% and a temperature of less than 25 °C. The storage period is 12 months, and the storage period is 5 months at 5-15 °C in a cool, low temperature and dry environment. It is best to keep away from odorous substances.

 

CERTIFICATE OF ANALYSIS

 

Packaging and storage

Solid food packaging bag, 25 kg / barrel.

 

Pepsin should be stored in dry, cool and well ventilated places away from the sun, heat.

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