Physical properties of Pepsin:
Pepsin powder is white or yellowish powder; No mildew and odor; There is moisture absorption; Acidic reaction of aqueous solution. Optimum temperature is 37℃/ optimum PH is 2.
Specific rotation: D26-64.5 (water pH 4.6).
Density: 1.287g/cm3
Storage conditions:-20 C.
Solubility: 10mMHCl: soluble, 1.0mg/mL, clear to slightly turbid and colorless.
Form: powder
Color: slightly beige
Odor: odorless
Water solubility: soluble in water and diligent aqueous buffers.
Sensitivity: Hygroscopic
Merck:13,7225
Stability: stable. Incompatible with strong alkali, alkali, metal salt and alcohol.
CAS database: 9001-75-6
What is Pepsin:
1. The enzyme that decomposes protein in gastric juice, also known as gastrin, is a substance containing protease, which is obtained from the fresh stomach of cattle or dolphins and can help the digestion of the stomach. It is a digestive protease. The main cellular function of gastric mucosa in the stomach is to decompose protein in food into small peptide fragments, and the main cell secretes pepsinogen, which is stimulated by gastric acid or pepsin to form pepsin, but pepsin is not directly produced by cells.
2. Pepsin powder is an enzyme that can promote protein digestion in food, and its premise is that pepsinogen is secreted by the main cells in the stomach. Under the action of gastric acid, pepsinogen can form pepsin to digest protein in food. For patients with gastritis and gastric ulcer, the lack of pepsinogen in the body is mainly due to the low content of gastric acid, which can not transform pepsinogen, thus affecting the digestion and absorption of protein, resulting in indigestion, bloating, acid regurgitation, burping and other symptoms.
3. Pepsin is a protease secreted by the main cells of the gastric gland, which has the ability to hydrolyze protein, with a molecular weight of 35,000 A, and is commonly used in protein to hydrolyze food products, pharmaceutical raw materials, food additives and other fields.
4. Pepsin is the main digestive enzyme in gastric juice, which is synthesized by amino acids in the main cells of gastric glands. When digesting food, pepsin is discharged into the gastric cavity to participate in digestion, and when digestion stops, it is synthesized again to supplement consumption, so that pepsin can always have sufficient grain reserves. Pepsin is the "main force" to digest food. However, it is not pepsin that is initially discharged from the main cell, but its precursor-pepsinogen. If pepsin is a knife, pepsinogen is like a knife with a scabbard, which has no digestive function. However, once it encounters an old partner-gastric acid and a little pepsin, it is like a knife drawn out, and immediately becomes pepsin with digestive function, becoming a "fresh force" for digesting food, and "combatively" digests all kinds of protein in food and hydrolyzes all peptide bond points in protein molecules, and protein becomes a simple structure. Pepsin and gastric acid are typical "iron buddies", they are both products of gastric mucosa glands, although the subtle parts are different; Proteinogen is activated by gastric acid; Protein treated with gastric acid, pepsin is the most labor-saving to digest; Gastric acid provides the most suitable working environment for pepsin; The content of pepsin is the "mirror" of the level of gastric acid, and the two are "inseparable". One is lacking, the other is often insufficient, and vice versa.
What is the function of pepsin? Introduce pepsin


What is the activation process of Pepsin?
Pepsin powder is first expressed as zymogen, that is, pepsinogen. Pepsinogen is an inactive precursor of pepsin, and its primary structure has 44 amino acids more than pepsin. In the stomach, pepsinogen is released from the main cells of gastric mucosa. This proenzyme is activated when it meets hydrochloric acid in gastric acid (released by gastric parietal cells). When the stomach digests food, pepsinogen and hydrochloric acid are released from the stomach wall under the action of a hormone called gastrin and vagus nerve. In the acidic environment created by hydrochloric acid, pepsinogen is unfolded, so that it can be used as
Autocatalysis shears itself, thus producing active pepsin. Subsequently, the generated pepsin continued to cut pepsinogen, cutting off 44 amino acid residues and producing more pepsin. This mechanism of maintaining the form of zymogen when there is no food digestion prevents excessive pepsin from digesting the stomach wall itself, which is a protective mechanism.
Product Specification
| Item | Specification | Result |
| Appearance | A white or slightly yellow powder | slightly yellow powder |
| Identification | conforms | conforms |
| Solubility | soluble in water, insoluble in alcohol and ether | Pass |
| Loss on drying | <5.0% | 0.036 |
| Sulphated Ash | <5.0% | 0.044 |
| Protease activity | ≥1:10000u/g | 1:11070u/g |
| Heavy metals | <20ppm | <20ppm |
| Total bacteria count | <5000 piece /g | <5000 piece /g |
| Yeast and Moulds | <100piece /g | <100piece /g |
| Escherichia Coli | Negative | Negative |
| Salmonella | Negative | Negative |
| PS.Aeruginosa | Negative | Negative |
| S.Aureus | Negative | Negative |
| Conclusion | Conform with enterprise specification . |
How is pepsin extract?
There are two main extraction methods of pepsin: acid extraction and alkali extraction.
Among them, acid extraction is relatively simple, but the activated pepsin is extracted, which has low stability. The pepsinogen that has not been activated is extracted by alkaline method, and the obtained protein is relatively stable, but the extraction time is long and there are many miscellaneous proteins.
Nevertheless, most of the known pepsin is extracted by alkaline method, which is beneficial to the study of the activation properties of zymogen and its long-term preservation.
At present, the mature processes for separating and purifying pepsin are as follows: 1. Leaching; 2. salting out and precipitation, which can be supplemented by membrane separation method; 3. Ion exchange chromatography and gel filtration chromatography. The crude enzyme solution is generally separated by salting-out precipitation method, supplemented by ultrafiltration membrane separation to remove salt and most impurities, and at the same time, the purpose of concentration can be achieved. Next, the method of combining gel column and ion exchange column was used for further purification, and the purity of pepsin could be above 95%.
Characterization atlas of Pepsin


What is the preparation process of pepsin (from pig)?
Grate sheep and bovine testis, extract acetic acid and hydrochloric acid, and salting out ammonium sulfate by stages.
Secondary salting out, ammonium sulfate dialysis, buffer solution to remove heat source, sodium phosphate, calcium acetate
Filter and dry the finished product.
The frozen testis of sheep and cattle was cut with a knife, and the inner and outer cortex and accessory testis were stripped and ground into chyme. Weigh 100kg of the slurry and pour it into the prepared cold acetic acid solution (90kg of water, 600ml of glacial acetic acid, and 10L of 1mol/L hydrochloric acid), stir vigorously at -5℃ for 3 ~ 4 min, then stir every 5min and extract for 4 h.. Then filter to obtain 125-140 l of extract. The pulp residue is extracted for the second time, and the amount of acid solution extracted is 1/3 of the first time, and the extractive solutions are combined. Under constant stirring, 210g of ammonium sulfate was added to each liter of the extract, and after it was completely dissolved, it was allowed to stand for about 1 hour, and filtered overnight with polyester cloth to obtain 110L of filtrate. Then, 290g of ammonium sulfate was added to each liter of filtrate to completely dissolve it, and then it was allowed to stand for 1 hour and filtered overnight to obtain crude hyaluronidase. Dissolve the crude product in 5L cold distilled water, add 125g ammonium sulfate under stirring to completely dissolve it, and leave it at 10℃ overnight. Remove the fat on the liquid surface, siphon off the supernatant and filter. The filtrate was continuously stirred, and then 750g of ammonium sulfate was slowly added to completely dissolve it, and it was left overnight at about 10℃. The next day, the supernatant was sucked to get the salting-out product. Dissolve the salted-out substance in 500ml cold distilled water, put it into dialysis bag, put it in 25L phosphate citric acid buffer solution with pH = 65 (citric acid 75g, Na2HPO4 12H2O 60g, sodium chloride 70g, made up with water to 2500ml, adjusted with citric acid to pH=6.5), dialyze at about 10℃ for 24h, and then filter to obtain dialysate. Cooling the dialysate in an ice bath, adding 50ml of 15%Na2HPO4·12H2O solution, slowly adding 30ml of 20% calcium acetate monohydrate solution under constant stirring, adjusting the pH value to 8.5 with 0.5mol/L sodium hydroxide solution, continuing stirring for 10min, filtering under reduced pressure, adjusting the pH value of the filtrate to 7.0 with 0.5 mol/L hydrochloric acid, and freeze-drying to obtain pyrogen-free glass. The yield is more than 2×104 units per kilogram of testis.
Where is pepsin used?
Commercial pepsin is extracted from the glandular layer of pig stomach. It is a component of rennet, which is used to coagulate milk during cheese production. Pepsin has many applications in food manufacturing: modifying soybean protein and gelatin to provide whipping quality, [40] modifying vegetable protein for non-dairy snack items, making pre-cooked cereals into instant hot cereals, [41] and preparing animal and vegetable protein hydrolysates for flavoring food and beverages. In leather industry, it is used to remove hair and residual tissues from hides, and to recover silver from discarded photographic films by digesting gelatin layers containing silver. [42] Historically, pepsin was an additive of Beaman chewing gum brand produced by Dr. Edwin E. Beaman.
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