Pepsin (Porcine Pepsin A)
Enzyme Preparations
9001-75-6
$21.71 ~ $32.56
Food
Free sample from 100g(NF)
One unit of:10kg/carton
One unit of:10kg/carton
10kg/carton
Product Info
What is Pepsin (Porcine Pepsin A)?
Pepsin (Porcine Pepsin A) is a naturally occurring protease enzyme derived from pig stomach, primarily used to break down proteins in digestion or food processing, such as clotting milk for cheese.
How is Pepsin (Porcine Pepsin A) made?
| Step No. | Production Stage | Key Action | Control Point & Note |
|---|---|---|---|
| 1 | Raw Material Sourcing | Collect fresh or frozen porcine (pig) gastric mucosa from approved, inspected abattoirs. | Source Integrity: Must be from healthy, veterinary-inspected pigs fit for human consumption. Handling: Rapid chilling or freezing is critical to prevent spoilage and loss of precursor activity. Full traceability of the source material is mandatory. |
| 2 | Extraction & Activation | Mince the stomach linings and place them in an acidified water solution (e.g., dilute HCl). This acidic environment extracts the pepsinogen and activates it into pepsin. | pH Control: The pH must be strictly maintained between 1.5 and 2.5 for efficient extraction and autocatalytic activation. Temperature: The process must be kept cold (e.g., below 10°C) to prevent protein denaturation and preserve enzyme activity. |
| 3 | Clarification & Filtration | Separate the acidic liquid extract from insoluble fats and tissue debris using centrifugation followed by multi-stage filtration. | Clarity: The efficiency of solid-liquid separation is crucial. A clear filtrate is required to ensure high purity in subsequent steps. Filter aids like diatomaceous earth may be used. |
| 4 | Purification by Precipitation | Selectively precipitate the pepsin from the clarified extract by adding a high concentration of a salt, such as sodium chloride ("salting out"). | Salt Concentration: The amount of salt added is precisely calculated to cause pepsin to precipitate while leaving other soluble protein impurities in the solution. This is a primary purification step. |
| 5 | Crude Collection & Washing | Collect the precipitated pepsin paste via centrifugation or filtration. Wash the paste with a chilled salt solution to remove impurities. | Purity Check: The washing step is vital for removing residual precipitating salts and other contaminants. The process is monitored to ensure thoroughness without re-dissolving the target enzyme. |
| 6 | Drying | Dry the purified pepsin paste under controlled low-temperature conditions, typically using vacuum drying or freeze-drying (lyophilization). | Drying Method: Freeze-drying is the preferred method as it is gentlest and best preserves the enzyme's three-dimensional structure and activity. Moisture Content: Final moisture must be controlled to a very low level (e.g., < 5%) for long-term stability. |
| 7 | Milling & Sieving | Mill the dried enzyme into a fine powder and pass it through sieves to achieve a uniform, specified particle size distribution. | Particle Size: This is controlled to meet customer requirements for characteristics like dissolvability and blendability. Heat generation during milling must be avoided. |
| 8 | Standardization & Blending | Accurately measure the enzymatic activity of the pure pepsin powder batch. Blend the powder with an inert, food-grade carrier (e.g., lactose or salt) to meet the final product's specified activity level. | Activity Assay: This is the most critical QC measurement, performed using a standardized pharmacopeial method (e.g., USP, NF, FCC). Homogeneity: The blending process must be validated to ensure the activity is uniform throughout the entire batch. |
| 9 | Final QC & Packaging | Perform a full panel of quality control tests on the final standardized product, including activity, microbial limits, heavy metals, and purity. Package in airtight, light- and moisture-proof containers. | Specification Compliance: The final batch must conform to all pre-defined specifications and relevant monograph requirements. Packaging: Proper packaging is essential to protect the enzyme's stability throughout its shelf life. Batches are clearly labeled with activity, lot number, and expiry date. |
Technical Specifications
| CAS Number | 9001-75-6 |
| Solubility | Soluble in water |
| Storage Conditions | Store dry, sealed; maintain 2–8 °C or cool room; avoid moisture |
| Shelf Life | 36 Months |
Applications & Usage
Common Applications:
protein digestion (food
pharmaceutical)
cheese making
gelatin hydrolysis
scientific assays
leather softening
Mechanism of action:
| Parameter | Pepsin (Porcine Pepsin A) |
|---|---|
| Functional Category | Enzyme; Protease; Processing Aid; Flavor Enhancer |
| Key Ingredients | Pepsin A (EC 3.4.23.1) derived from porcine stomach mucosa. |
| Mechanism of Action | Acts as an endopeptidase, specifically an aspartic protease, which cleaves internal peptide bonds within protein chains. It exhibits high specificity for peptide bonds involving aromatic amino acids (e.g., phenylalanine, tyrosine) and other large hydrophobic residues. Catalysis is optimal in highly acidic environments (pH 1.5-2.5), leading to the breakdown of large proteins into smaller polypeptides and peptones. |
| Application Effect in Product | Initiates casein coagulation in cheesemaking (as a rennet substitute); tenderizes meat by hydrolyzing collagen and myofibrillar proteins; produces protein hydrolysates for savory flavors and nutritional supplements; clarifies beverages (e.g., beer, fruit juice) by breaking down haze-forming proteins. |
Comparison:
| Product Name | Category/Type | Key Features | Strengths (vs peers) | Weaknesses (vs peers) | Best Use Cases | Why Choose |
|---|---|---|---|---|---|---|
| Pepsin (Porcine Pepsin A) | Animal-derived Aspartic Protease | Optimal activity at very low pH (1.5–2.5); derived from pig stomachs; cleaves peptide bonds adjacent to aromatic amino acids. | Extremely high activity in highly acidic conditions, mimicking the stomach. Well-established and highly characterized. | Inactive at neutral or alkaline pH. Animal source may not meet certain dietary (e.g., Halal, Kosher) or ethical requirements. | Digestive aid supplements, laboratory protein digestion, food processing (e.g., soy protein hydrolysis), collagen preparation. | When maximal proteolytic activity in a highly acidic environment is required, simulating gastric digestion. |
| Papain | Plant-derived Cysteine Protease | Derived from papaya latex; active over a very broad pH range (3–9); broad substrate specificity. | Functions across a wide pH range, making it versatile. Plant-based (vegan, widely acceptable). Readily available. | Less specific than pepsin. Can impart a slight flavor in food applications. Its broad action can lead to over-tenderizing. | Meat tenderizing, beer chill-proofing, dietary supplements, wound debridement applications. | For a versatile, plant-based enzyme that works in both acidic and neutral conditions. |
| Bromelain | Plant-derived Cysteine Protease | Derived from pineapple; active over a broad pH range (4–8); known for both digestive and anti-inflammatory properties. | Plant-based. Offers dual benefits as a digestive aid and for inflammation support. Effective tenderizer. | Less active than pepsin in extremely acidic conditions. Activity can vary based on source (stem vs. fruit). | Dietary supplements (digestion, inflammation), meat tenderizing, food processing, cosmetic applications. | For a plant-based option, especially in supplements where anti-inflammatory benefits are also desired. |
| Fungal Acid Protease | Microbial-derived Aspartic Protease | Produced via fermentation (e.g., from *Aspergillus niger*); optimal activity at low pH (2.5–4.0). | Non-animal source (vegan, Halal, Kosher). High consistency and scalability from fermentation. Cost-effective. | Optimal pH range is typically not as low as porcine pepsin. Specificity can differ. | Baking (dough conditioning), animal feed, brewing, beverage clarification, industrial-scale protein modification. | A scalable, cost-effective, and non-animal alternative for industrial applications requiring acidic proteolysis. |
| Rennet (Chymosin) | Animal or Microbial Aspartic Protease | Highly specific for cleaving kappa-casein in milk, causing coagulation. Optimal at slightly acidic to neutral pH (6.0-6.5). | Unmatched specificity and efficiency for milk clotting in cheesemaking, leading to better curd and yield. | Very narrow application scope; ineffective for general protein digestion. Animal source (calf) has ethical/cost concerns. | Cheesemaking and production of casein-based products. | The definitive choice for cheesemaking, where specific milk coagulation is the primary and essential function. |
| Trypsin | Animal-derived Serine Protease | Optimal activity at alkaline pH (7.5–8.5); highly specific cleavage after Lysine or Arginine residues. | Functions in alkaline environments where pepsin is inactive. High specificity is crucial for research applications. | Completely inactive in acidic conditions. Functionally opposite to pepsin in a digestive context (duodenum vs. stomach). | Cell culture (detaching cells), proteomics (protein sequencing), infant formula production, pharmaceutical applications. | For lab or industrial use requiring highly specific protein cleavage in an alkaline environment. Not a pepsin alternative. |
Technical Documents
Available Documentation
Spec sheet, activity assay report, MSDS available
Safety Data Sheet (SDS)
Available
Certificate of Analysis (COA)
Quality assurance documentation
Technical Data Sheet
Detailed technical specifications