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Home > Products >  China Largest Manufacturer factory sales pepsin CAS 9001-75-6

China Largest Manufacturer factory sales pepsin CAS 9001-75-6 CAS NO.9001-75-6

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  • Min.Order: 500 Kilogram
  • Payment Terms: L/C,D/A,D/P,T/T,MoneyGram,Other
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    AAAAA(50-100)KilogramAAAAA(100-500)Kilogram

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Keywords

  • pepsin
  • pepsin
  • 9001-75-6

Quick Details

  • ProName: China Largest Manufacturer factory sal...
  • CasNo: 9001-75-6
  • Molecular Formula: 9001-75-6
  • Appearance: white powder
  • Application: Pharm chemicals industry
  • DeliveryTime: 3-5 days
  • PackAge: 25KG/Drum
  • Port: Shanghai Guangzhou Qingdao Shenzhen
  • ProductionCapacity: 20 Metric Ton/Month
  • Purity: 99%
  • Storage: 2-8°C
  • Transportation: By air /Sea/ coruier
  • LimitNum: 500 Kilogram
  • Heavy metal: 10PPM
  • Color: red
  • Melting point: ≥350°C
  • Boiling point: 363.24°C (rough estimate)
  • density: 1.667
  • solubility: 1 M NaOH: 10 mg/mL, dark green
  • Water Solubility: <0.1 g/100 mL at 21 oC
  • Stability: Stable. Combustible. Incompatible with...

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                                PRODUCT DETAILS                           

Pepsin Basic information
Overview Biological location and functions Factor affecting the activity of pepsin Applications References
Product Name: Pepsin
Synonyms: IMMOBILIZED PEPSIN;Pepsine from porcine (high activity, 1: 50000) lyophil.;Pepsin ,>0.7 Ph.Eur.U/Mg (activity);OMniTrace Ultra (TM) Perchloric Acid;Pepsin(porcine stoMach Mucose);BOVINEPEPSINB;AVIANPEPSIN;BOVINEPEPSINA
CAS: 9001-75-6
MF: n.a.
MW: 0
EINECS: 232-629-3
Product Categories: Enzymes;API
Mol File: Mol File
Pepsin Structure
 
Pepsin Chemical Properties
alpha  D26 -64.5° (water pH 4.6)
density  1.287 g/cm3
storage temp.  -20°C
solubility  10 mM HCl: soluble1.0mg/mL, clear to faintly turbid, colorless
form  powder
color  slightly beige
Odor Odorless
Water Solubility  Soluble in water and dilute aqueous buffers
Sensitive  Hygroscopic
Merck  13,7225
Stability: Stable. Incompatible with strong bases, alkalies, metallic salts, alcohols.
CAS DataBase Reference 9001-75-6
EPA Substance Registry System Pepsin A (9001-75-6)
 
Safety Information
Hazard Codes  Xn
Risk Statements  36/37/38-42-42/43
Safety Statements  22-24-26-36/37-36-45
WGK Germany  1
RTECS  SC6132000
3-10
TSCA  Yes
HS Code  35079090
MSDS Information
Provider Language
Pepsin English
 
Pepsin Usage And Synthesis
Overview Pepsin is a kind of endopeptidase that breaks down proteins into smaller peptides (that is, a protease). It is biologically produced in the animal stomach and is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an important acidic protease that is widely applied in the hydrolysis of proteins. It is used in collagen extraction[1-3] in gelatin extraction[4] as a rennet substitute[5] and in digestibility therapy[6]. Pepsin has been isolated and investigated from various mammals including: human, Japanese monkey, pig, bovine, goat, rat, and rabbit. Pepsin can be found primarily in the gastric juice of the stomach lumen and can be isolated from a variety of species such as human, cattles, sheeps, birds and fish[7,8]. The main location of pepsin in mammals is the stomach (both the membrane and the gastric juice) but it can also be found in limited amounts in the blood, muscle and the urine[7].
There are several types of stomach pepsins, each has a distinct protein structure and enzymatic properties[9]. Pepsin has a three-dimensional structure, of which one or more polypeptide chains twist and fold, bringing together a small number of amino acids to form the active site, or the location on the enzyme where the substrate binds and the reaction takes place. Pepsin is an aspartic protease, using a catalytic aspartate in its active site[10].
Biological location and functions Pepsin is synthesized and secreted in the gastric membrane in an inactive state called pepsinogen (PG) (molecular weight of 40kDa). Compared with pepsin, pepsinogen contains an additional 44 amino acids and is stable in neutral and weak alkaline environments, but when exposed to the hydrochloric acid (HCl) present in gastric juice (pH of 1.5 – 2.0), the 44 amino acids are proteolytically removed in an autocatalytic way to activate it to pepsin[11]. Its main role in protein proteolysis is to cleave aromatic amino acids (such as phenylalanine and tyrosine) from the N–terminus of proteins[11].
Pepsin is one of three principal proteases in the human digestive system with the other two being chymotrypsin and trypsin. During the process of digestion in the digestive system, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the small intestine. Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine12. Pepsin's proenzyme, pepsinogen, is released by the chief cells in the stomach wall, and upon mixing with the hydrochloric acid of the gastric juice, pepsinogen activates to become pepsin13.
Factor affecting the activity of pepsin The activity of pepsin can be strongly affected by pH, temperature and inhibitors.
pH
Both the optimum pH (the pH value giving the highest enzymatic activity) and pH stability (the pH range giving good enzyme stability) have significant effects on the activity of pepsin. When the pH deviates from the optimum value, the activity of pepsin drops. Generally, pepsin stability is mentioned at lower pH values. Pepsin is a type of acidic protease and depression of its stability is attributed to the denaturation of proteins above the pH of 6.0. Study has found that the stability and activity of pepsin showed that 70% of maximal peptic activity was present at pH4.5 and that pepsin was irreversibly inactivated at pH 8[14]. Pepsin exhibits maximal activity at pH 2.0 and is inactive at pH 6.5 and above[15, 16].
Temperature
Temperature has a great influence on the activity of pepsin. Like pH, the optimum temperature and thermal stability range are very important. Pepsin is most active in acidic environments between 37 °C and 42 °C[17].
Inhibitors
Pepstatin A (a typical aspartic proteinase inhibitor) can combine with pepsin and prevents the binding of the enzyme to substrate, thereby resulting in a complete inhibition of its activity.
Pepstatin A is a peptide isolated from several species of actinomyces, such as Streptomyces spp. It has one of the lowest known inhibitions constant (Ki= 45 pM) for pepsin[18, 19].
Applications Medical research
Pepsin is utilized in regulation of digestion, as a dental antiseptic and in treatment of ailment including dyspepsia, gastralgia, obstinate vomiting, infantile diarrhea, apepsia and some cancer[5]. Combined with HCl, pepsin tablets and capsules have been developed to support the digestibility in the gastrointestinal tract as well as to enhance the appetite of patients [6]. Pepsin from porcine stomach is used for treatment of gastric ulcers with bismuth complexes added[7]. Pepsin is also added for better digestibility of proteins in animals feed.
Pepsin is also commonly used in the preparation of F(ab')2 fragments from antibodies [23].
Cheese making
Animal (calf, bovine and porcine sources) rennet is composed of pepsin and chymosin commonly mixed in a ratio of 1:9 and used in commercial cheese making. During the food manufacturing process, pepsin is very useful in: modifying and providing whipping qualities to soy protein and gelatin, modifying vegetable proteins for use in nondairy snack items, making precooked cereals into instant hot cereals, and preparing animal and vegetable protein hydrolysates for use in flavoring foods and beverages[24].
Collagen extraction
Conventionally, collagen is extracted by an acid-solubilization process (ASP) in which collagen is solubilized in an acid (such as acetic acid) and other non-acid-soluble materials are removed. Since pepsin can break down cross-linkages in the telo peptide regions of collagen without harming to its secondary structure, the use of pepsin in this process can effectively enhance the yield of collagen[25].
Purification
The process of partitioning of pepsin commonly involves three steps: (a) extraction of pepsinogen which involves preparation of stomach and crude extract, (b) purification of pepsinogen and (c) activation of pepsinogen to pepsin. All these steps are conducted at low temperatures (≤ 4ºC) to prevent denaturation of proteins[26].
References
  1. Jongjareonrak A, Benjakul S, Visessanguan W, Nagai T, Tanaka M (2005) Isolation and characterisation of acid and pepsin–solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta). Food Chem 93: 475-484.
  2. Zhang Y, Liu W, Li G, Shi B, Miao Y, et al. (2007) Isolation and partial characterization of pepsin-soluble collagen from the skin of grass carp (Ctenopharyngodon idella). Food Chem 103: 906-912.
  3. Nalinanon S, Benjakul S, Visessanguan W, Kishimura H (2007) Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthustayenus). Food Chem104: 593-601.
  4. Nalinanon S, Benjakul S, Visessanguan W, Kishimura H (2008) Improvement of gelatin extraction from bigeye snapper skin using pepsin-aided process in combination with protease inhibitor. Food Hydrocolloids 22: 615-622.
  5. Aehle W (2007) Enzymes in industry: production and applications. (3rdedn), Wiley–VCH, Weinheim, Germany, 136-137.
  6. Thorne Research (2010) Betaine HCl and Pepsin; Dover, USA. Sogawa K, Fujii–Kuriyama Y, Mizukami Y, Ichihara Y, Takahashi T (1983) Primary structure of human pepsinogen gene. J Biol Chem 258: 5306-5311.
  7. Fruton JS (1971) Hydrolysis: peptide bonds, (3rd edn), Academic Press Inc: New York 3: 120-152.
  8. Effront J, Prescott SC, Venable CS (2007) Biochemical catalysts in life and industry: proteolytic enzymes. Kessinger Publishing: 151-289.
  9. Shahidi F, Janak Kamil YVA (2001) Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci Technol 12: 435-464.
  10. #
  11. Raufman J (2004) Pepsin. In Encyclopedia of Gastroenterology, Johnson L R. Ed., Academic Press, Amsterdam 3: 147-148.
  12. #
  13. Kageyama, T, and K. Takahashi. "Occurrence of two different pathways in the activation of porcine pepsinogen to pepsin." Journal of Biochemistry 93.3(1983):743-754.
  14. Piper, D. W., and B. H. Fenton. "pH stability and activity curves of pepsin with special reference to their clinical importance." Gut 6.5(1965): 506-508.
  15. Squires EJ, Haard NF, Feltham LA (1986) Gastric proteases of the Greenland cod Gadus ogac. I. Isolation and kinetic properties. Biochem Cell Biol 64: 205-214.
  16. Johnston N, Dettmar PW, Bishwokarma B, Lively MO, Koufman JA (Jun 2007). "Activity/stability of human pepsin: implications for reflux attributed laryngeal disease". The Laryngoscope. 117 (6): 1036–9.
  17. #
  18. Umezawa H, Aoyagi T, Morishima H, Matsuzaki M, Hamada M (1970) Pepstatin, a new pepsin inhibitor produced by agtinomygetes. J Antibiot (Tokyo) 23: 259-262.
  19. Zollner H (1999) Handbook of enzyme inhibitors. (3thedn), Wiley–VCH, Chichester, UK, 440-445.
  20. Gorgas FJS (2009) Dental medicine. A manual of dental material medica and therapeutics, Nabu Press, Washington, 48-50.
  21. Murado MA, González MDP, Vázquez JA (2009) Recovery of proteolytic and collagenolytic activities from viscera by-products of rayfish (Raja clavata). Mar Drugs 7: 803-815.
  22. Almås KA (1990) Utilization of marine biomass for production of microbial growth media and biochemicals. In Advances in Fisheries Technology and Biotechnology for increased profitability, Voigt MN, Botta JR, Eds., Technomic Publishing Company, Lamcaster, 361-372.
  23. Falkenburg WJ, van Schaardenburg D, Ooijevaar-de Heer P, Tsang-A-Sjoe MW, Bultink IE, Voskuyl AE, Bentlage AE, Vidarsson G, Wolbink G, Rispens T (2016). "Anti-Hinge Antibodies Recognize IgG Subclass- and Protease-Restricted Neoepitopes". Journal of Immunology.
  24. Kun LY (2006). Microbial Biotechnology: Principles And Applications. World Scientific Publishing Company. 
  25. Jongjareonrak A, Benjakul S, Visessanguan W, Nagai T, Tanaka M (2005) Isolation and characterisation of acid and pepsin–solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta). Food Chem 93: 475-484.
  26. Roe SD (2001) Purification strategy. In Protein purification techniques (2ndedn), Roe S, Eds, Oxford University Press Inc, New York, 1-10.
Chemical Properties White or slightly yellow, crystalline or amorphous powder, hygroscopic.
Uses Proteolytic enzyme.
Uses Pepsin is an enzyme that is secreted in the digestive track of mammals. It works to break down proteins into smaller peptides which can readily be absorbed by the small intestine.
Definition An enzyme that catalysesthe breakdown of proteins topolypeptides in the vertebrate stomach.It is secreted as an inactive precursor,pepsinogen.
General Description

Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep.

Biochem/physiol Actions Unlike many other peptidases, pepsin hydrolyzes only peptide bonds, not amide or ester linkages. The cleavage specificity includes peptides with an aromatic acid on either side of the peptide bond, especially if the other residue is also an aromatic or a dicarboxylic amino acid. Increased susceptibility to hydrolysis occurs if there is a sulfur-containing amino acid close to the peptide bond, which has an aromatic amino acid. Pepsin will also preferentially cleave at the carboxyl side of phenylalanine and leucine, and to a lesser extent at the carboxyl side of glutamic acid residues. It does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.
Purification Methods Pepsin is re-chromatographed on a column of Amberlite CG-50 using a pH gradient prior to use. Crystallise it from EtOH. [Richmond et al. Biochim Biophys Acta 29 453 1958, Huang & Tang, J Biol Chem 244 1085 1969, 245 2189 1970.]
 
Pepsin Preparation Products And Raw materials
Raw materials Sucrose-->Lactose-->HEROIN-->Saccharated Pepsin-->HISTONE
Preparation Products Gastric Mucin-->Gastrin I Human


                                                                       Group profiles


Leader Biochemical Group is a large leader incorporated industry manufacturers and suppliers of advanced refined raw materials From the year of 1996 when our factory was put into production to year of 2020, our group has successively invested in more than 52 factories with shares and subordinates.We focus on manufacture Pharm & chemicals, functional active ingredients, nutritional Ingredients, health care products, cosmetics, pharmaceutical and refined feed, oil, natural plant ingredients industries to provide top quality of GMP standards products.All the invested factories' product lines cover API and intermediates, vitamins, amino acids, plant extracts, daily chemical products, cosmetics raw materials, nutrition and health care products, food additives, feed additives, essential oil products, fine chemical products and agricultural chemical raw materials And flavors and fragrances. Especially in the field of vitamins, amino acids, pharmaceutical raw materials and cosmetic raw materials, we have more than 20 years of production and sales experience. All products meet the requirements of high international export standards and have been recognized by customers all over the world. Our manufacture basement & R&D center located in National Aerospace Economic & Technical Development Zone Xi`an Shaanxi China. Now not only relying on self-cultivation and development as well as maintains good cooperative relations with many famous research institutes and universities in China. Now, we have closely cooperation with Shanghai Institute of Organic Chemistry of Chinese Academy of Science, Beijing Institute of Material Medical of Chinese Academy of Medical Science, China Pharmaceutical University, Zhejiang University. Closely cooperation with them not only integrating Science and technology resources, but also increasing the R&D speed and improving our R&D power. Offering Powerful Tech supporting Platform for group development. Keep serve the manufacture and the market as the R&D central task, focus on the technical research.  Now there are 3 technology R & D platforms including biological extract, microorganism fermentation and chemical synthesis, and can independently research and develop kinds of difficult APIs and pharmaceutical intermediates. With the strong support of China State Institute of Pharmaceutical Industry (hereinafter short for CSIPI), earlier known as Shanghai Institute of Pharmaceutical Industry (SIPI), we have unique advantages in the R & D and industrialization of high-grade, precision and advanced products.  Now our Group technical force is abundant, existing staff more that 1000 people, senior professional and technical staff accounted for more than 50% of the total number of employees, including 15 PhD research and development personnel, 5 master′ S degree in technical and management personnel 9 people. We have advanced equipment like fermentation equipment and technology also extraction, isolation, purification, synthesis with rich production experience and strict quality control system, According to the GMP required, quickly transforming the R&D results to industrial production in time, it is our advantages and our products are exported to North and South America, Europe, Middle East, Africa, and other five continents and scale the forefront in the nation, won good international reputation.  We believe only good quality can bring good cooperation, quality is our key spirit during our production, we are warmly welcome clients and partner from all over the world contact us for everlasting cooperation, Leader will be your strong, sincere and reliable partner in China.

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                                                       Product information

Pepsin Basic information
Overview Biological location and functions Factor affecting the activity of pepsin Applications References
Product Name: Pepsin
Synonyms: IMMOBILIZED PEPSIN;Pepsine from porcine (high activity, 1: 50000) lyophil.;Pepsin ,>0.7 Ph.Eur.U/Mg (activity);OMniTrace Ultra (TM) Perchloric Acid;Pepsin(porcine stoMach Mucose);BOVINEPEPSINB;AVIANPEPSIN;BOVINEPEPSINA
CAS: 9001-75-6
MF: n.a.
MW: 0
EINECS: 232-629-3
Product Categories: Enzymes;API
Mol File: Mol File
Pepsin Structure
 
Pepsin Chemical Properties
alpha  D26 -64.5° (water pH 4.6)
density  1.287 g/cm3
storage temp.  -20°C
solubility  10 mM HCl: soluble1.0mg/mL, clear to faintly turbid, colorless
form  powder
color  slightly beige
Odor Odorless
Water Solubility  Soluble in water and dilute aqueous buffers
Sensitive  Hygroscopic
Merck  13,7225
Stability: Stable. Incompatible with strong bases, alkalies, metallic salts, alcohols.
CAS DataBase Reference 9001-75-6
EPA Substance Registry System Pepsin A (9001-75-6)
 
Safety Information
Hazard Codes  Xn
Risk Statements  36/37/38-42-42/43
Safety Statements  22-24-26-36/37-36-45
WGK Germany  1
RTECS  SC6132000
3-10
TSCA  Yes
HS Code  35079090
MSDS Information
Provider Language
Pepsin English
 
Pepsin Usage And Synthesis
Overview Pepsin is a kind of endopeptidase that breaks down proteins into smaller peptides (that is, a protease). It is biologically produced in the animal stomach and is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an important acidic protease that is widely applied in the hydrolysis of proteins. It is used in collagen extraction[1-3] in gelatin extraction[4] as a rennet substitute[5] and in digestibility therapy[6]. Pepsin has been isolated and investigated from various mammals including: human, Japanese monkey, pig, bovine, goat, rat, and rabbit. Pepsin can be found primarily in the gastric juice of the stomach lumen and can be isolated from a variety of species such as human, cattles, sheeps, birds and fish[7,8]. The main location of pepsin in mammals is the stomach (both the membrane and the gastric juice) but it can also be found in limited amounts in the blood, muscle and the urine[7].
There are several types of stomach pepsins, each has a distinct protein structure and enzymatic properties[9]. Pepsin has a three-dimensional structure, of which one or more polypeptide chains twist and fold, bringing together a small number of amino acids to form the active site, or the location on the enzyme where the substrate binds and the reaction takes place. Pepsin is an aspartic protease, using a catalytic aspartate in its active site[10].
Biological location and functions Pepsin is synthesized and secreted in the gastric membrane in an inactive state called pepsinogen (PG) (molecular weight of 40kDa). Compared with pepsin, pepsinogen contains an additional 44 amino acids and is stable in neutral and weak alkaline environments, but when exposed to the hydrochloric acid (HCl) present in gastric juice (pH of 1.5 – 2.0), the 44 amino acids are proteolytically removed in an autocatalytic way to activate it to pepsin[11]. Its main role in protein proteolysis is to cleave aromatic amino acids (such as phenylalanine and tyrosine) from the N–terminus of proteins[11].
Pepsin is one of three principal proteases in the human digestive system with the other two being chymotrypsin and trypsin. During the process of digestion in the digestive system, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the small intestine. Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine12. Pepsin's proenzyme, pepsinogen, is released by the chief cells in the stomach wall, and upon mixing with the hydrochloric acid of the gastric juice, pepsinogen activates to become pepsin13.
Factor affecting the activity of pepsin The activity of pepsin can be strongly affected by pH, temperature and inhibitors.
pH
Both the optimum pH (the pH value giving the highest enzymatic activity) and pH stability (the pH range giving good enzyme stability) have significant effects on the activity of pepsin. When the pH deviates from the optimum value, the activity of pepsin drops. Generally, pepsin stability is mentioned at lower pH values. Pepsin is a type of acidic protease and depression of its stability is attributed to the denaturation of proteins above the pH of 6.0. Study has found that the stability and activity of pepsin showed that 70% of maximal peptic activity was present at pH4.5 and that pepsin was irreversibly inactivated at pH 8[14]. Pepsin exhibits maximal activity at pH 2.0 and is inactive at pH 6.5 and above[15, 16].
Temperature
Temperature has a great influence on the activity of pepsin. Like pH, the optimum temperature and thermal stability range are very important. Pepsin is most active in acidic environments between 37 °C and 42 °C[17].
Inhibitors
Pepstatin A (a typical aspartic proteinase inhibitor) can combine with pepsin and prevents the binding of the enzyme to substrate, thereby resulting in a complete inhibition of its activity.
Pepstatin A is a peptide isolated from several species of actinomyces, such as Streptomyces spp. It has one of the lowest known inhibitions constant (Ki= 45 pM) for pepsin[18, 19].
Applications Medical research
Pepsin is utilized in regulation of digestion, as a dental antiseptic and in treatment of ailment including dyspepsia, gastralgia, obstinate vomiting, infantile diarrhea, apepsia and some cancer[5]. Combined with HCl, pepsin tablets and capsules have been developed to support the digestibility in the gastrointestinal tract as well as to enhance the appetite of patients [6]. Pepsin from porcine stomach is used for treatment of gastric ulcers with bismuth complexes added[7]. Pepsin is also added for better digestibility of proteins in animals feed.
Pepsin is also commonly used in the preparation of F(ab')2 fragments from antibodies [23].
Cheese making
Animal (calf, bovine and porcine sources) rennet is composed of pepsin and chymosin commonly mixed in a ratio of 1:9 and used in commercial cheese making. During the food manufacturing process, pepsin is very useful in: modifying and providing whipping qualities to soy protein and gelatin, modifying vegetable proteins for use in nondairy snack items, making precooked cereals into instant hot cereals, and preparing animal and vegetable protein hydrolysates for use in flavoring foods and beverages[24].
Collagen extraction
Conventionally, collagen is extracted by an acid-solubilization process (ASP) in which collagen is solubilized in an acid (such as acetic acid) and other non-acid-soluble materials are removed. Since pepsin can break down cross-linkages in the telo peptide regions of collagen without harming to its secondary structure, the use of pepsin in this process can effectively enhance the yield of collagen[25].
Purification
The process of partitioning of pepsin commonly involves three steps: (a) extraction of pepsinogen which involves preparation of stomach and crude extract, (b) purification of pepsinogen and (c) activation of pepsinogen to pepsin. All these steps are conducted at low temperatures (≤ 4ºC) to prevent denaturation of proteins[26].
References
  1. Jongjareonrak A, Benjakul S, Visessanguan W, Nagai T, Tanaka M (2005) Isolation and characterisation of acid and pepsin–solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta). Food Chem 93: 475-484.
  2. Zhang Y, Liu W, Li G, Shi B, Miao Y, et al. (2007) Isolation and partial characterization of pepsin-soluble collagen from the skin of grass carp (Ctenopharyngodon idella). Food Chem 103: 906-912.
  3. Nalinanon S, Benjakul S, Visessanguan W, Kishimura H (2007) Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthustayenus). Food Chem104: 593-601.
  4. Nalinanon S, Benjakul S, Visessanguan W, Kishimura H (2008) Improvement of gelatin extraction from bigeye snapper skin using pepsin-aided process in combination with protease inhibitor. Food Hydrocolloids 22: 615-622.
  5. Aehle W (2007) Enzymes in industry: production and applications. (3rdedn), Wiley–VCH, Weinheim, Germany, 136-137.
  6. Thorne Research (2010) Betaine HCl and Pepsin; Dover, USA. Sogawa K, Fujii–Kuriyama Y, Mizukami Y, Ichihara Y, Takahashi T (1983) Primary structure of human pepsinogen gene. J Biol Chem 258: 5306-5311.
  7. Fruton JS (1971) Hydrolysis: peptide bonds, (3rd edn), Academic Press Inc: New York 3: 120-152.
  8. Effront J, Prescott SC, Venable CS (2007) Biochemical catalysts in life and industry: proteolytic enzymes. Kessinger Publishing: 151-289.
  9. Shahidi F, Janak Kamil YVA (2001) Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci Technol 12: 435-464.
  10. #
  11. Raufman J (2004) Pepsin. In Encyclopedia of Gastroenterology, Johnson L R. Ed., Academic Press, Amsterdam 3: 147-148.
  12. #
  13. Kageyama, T, and K. Takahashi. "Occurrence of two different pathways in the activation of porcine pepsinogen to pepsin." Journal of Biochemistry 93.3(1983):743-754.
  14. Piper, D. W., and B. H. Fenton. "pH stability and activity curves of pepsin with special reference to their clinical importance." Gut 6.5(1965): 506-508.
  15. Squires EJ, Haard NF, Feltham LA (1986) Gastric proteases of the Greenland cod Gadus ogac. I. Isolation and kinetic properties. Biochem Cell Biol 64: 205-214.
  16. Johnston N, Dettmar PW, Bishwokarma B, Lively MO, Koufman JA (Jun 2007). "Activity/stability of human pepsin: implications for reflux attributed laryngeal disease". The Laryngoscope. 117 (6): 1036–9.
  17. #
  18. Umezawa H, Aoyagi T, Morishima H, Matsuzaki M, Hamada M (1970) Pepstatin, a new pepsin inhibitor produced by agtinomygetes. J Antibiot (Tokyo) 23: 259-262.
  19. Zollner H (1999) Handbook of enzyme inhibitors. (3thedn), Wiley–VCH, Chichester, UK, 440-445.
  20. Gorgas FJS (2009) Dental medicine. A manual of dental material medica and therapeutics, Nabu Press, Washington, 48-50.
  21. Murado MA, González MDP, Vázquez JA (2009) Recovery of proteolytic and collagenolytic activities from viscera by-products of rayfish (Raja clavata). Mar Drugs 7: 803-815.
  22. Almås KA (1990) Utilization of marine biomass for production of microbial growth media and biochemicals. In Advances in Fisheries Technology and Biotechnology for increased profitability, Voigt MN, Botta JR, Eds., Technomic Publishing Company, Lamcaster, 361-372.
  23. Falkenburg WJ, van Schaardenburg D, Ooijevaar-de Heer P, Tsang-A-Sjoe MW, Bultink IE, Voskuyl AE, Bentlage AE, Vidarsson G, Wolbink G, Rispens T (2016). "Anti-Hinge Antibodies Recognize IgG Subclass- and Protease-Restricted Neoepitopes". Journal of Immunology.
  24. Kun LY (2006). Microbial Biotechnology: Principles And Applications. World Scientific Publishing Company. 
  25. Jongjareonrak A, Benjakul S, Visessanguan W, Nagai T, Tanaka M (2005) Isolation and characterisation of acid and pepsin–solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta). Food Chem 93: 475-484.
  26. Roe SD (2001) Purification strategy. In Protein purification techniques (2ndedn), Roe S, Eds, Oxford University Press Inc, New York, 1-10.
Chemical Properties White or slightly yellow, crystalline or amorphous powder, hygroscopic.
Uses Proteolytic enzyme.
Uses Pepsin is an enzyme that is secreted in the digestive track of mammals. It works to break down proteins into smaller peptides which can readily be absorbed by the small intestine.
Definition An enzyme that catalysesthe breakdown of proteins topolypeptides in the vertebrate stomach.It is secreted as an inactive precursor,pepsinogen.
General Description

Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep.

Biochem/physiol Actions Unlike many other peptidases, pepsin hydrolyzes only peptide bonds, not amide or ester linkages. The cleavage specificity includes peptides with an aromatic acid on either side of the peptide bond, especially if the other residue is also an aromatic or a dicarboxylic amino acid. Increased susceptibility to hydrolysis occurs if there is a sulfur-containing amino acid close to the peptide bond, which has an aromatic amino acid. Pepsin will also preferentially cleave at the carboxyl side of phenylalanine and leucine, and to a lesser extent at the carboxyl side of glutamic acid residues. It does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.
Purification Methods Pepsin is re-chromatographed on a column of Amberlite CG-50 using a pH gradient prior to use. Crystallise it from EtOH. [Richmond et al. Biochim Biophys Acta 29 453 1958, Huang & Tang, J Biol Chem 244 1085 1969, 245 2189 1970.]
 
Pepsin Preparation Products And Raw materials
Raw materials Sucrose-->Lactose-->HEROIN-->Saccharated Pepsin-->HISTONE
Preparation Products Gastric Mucin-->Gastrin I Human

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