Papain
Enzyme Preparations
9001-73-4
$8.75 ~ $13.12
Food
Free sample from 100g(NF)
One unit of:20kg/carton
One unit of:20kg/carton
20kg/carton
Product Info
What is Papain?
Papain is a proteolytic enzyme extracted from papaya, used mainly as a meat tenderizer and a clarifier in brewing and food processing.
How is Papain made?
| Step No. | Production Stage | Key Action | Control Point & Note |
|---|---|---|---|
| 1 | Latex Collection | Make shallow incisions (lancing) on the surface of unripe, mature green papaya fruits to collect the oozing milky latex. | Note: Collection is best done in the early morning for higher latex yield. The fruit must be unripe as papain activity decreases significantly upon ripening. Use clean, non-metallic containers. |
| 2 | Coagulation & Filtration | Allow the raw latex to coagulate and then filter it through a fine mesh to separate the liquid enzyme solution from solid impurities like fruit debris and rubbery components. | Control Point: This step must be performed quickly after collection to prevent microbial degradation and loss of enzyme activity. The filter size is key to a clean filtrate. |
| 3 | Purification & Precipitation | Add a precipitating agent (e.g., food-grade ethanol or ammonium sulfate) to the filtered liquid to selectively cause the papain enzyme to precipitate out of the solution. | Control Point: The process must be conducted at a low temperature (e.g., 4-10°C) to protect the enzyme from denaturation. The concentration of the precipitating agent is critical for efficiency. |
| 4 | Centrifugation | Separate the solid, precipitated papain paste from the liquid supernatant using a high-speed centrifuge. | Control Point: Centrifuge speed and time must be optimized to ensure maximum recovery of the enzyme paste and achieve a firm, solid pellet. |
| 5 | Drying | Dry the wet enzyme paste to a stable powder using methods like vacuum drying or spray drying. | Critical Control Point: The drying temperature must be kept low (typically below 60°C) to prevent thermal denaturation, which would irreversibly destroy the enzyme's activity. Final moisture content must be below 8%. |
| 6 | Milling & Sieving | Grind the dried, crude papain into a fine powder and pass it through sieves to achieve a uniform particle size. | Control Point: Milling process must be controlled to avoid generating excessive heat. Sieving ensures product homogeneity and meets customer specifications for solubility. |
| 7 | Standardization & Quality Control | Test the enzyme's proteolytic activity (e.g., in Milk Clotting Units - MCU). Blend the powder with an inert, food-grade carrier (like lactose or maltodextrin) to achieve a standardized activity level. | Critical Control Point: The enzymatic activity assay is the most important QC test. The final product must also be tested for microbiological purity (e.g., E. coli, Salmonella) and heavy metals. |
| 8 | Packaging | Package the final, standardized papain powder into sealed, airtight, and moisture-proof containers. | Note: Packaging must protect the enzyme from moisture, oxygen, and light, all of which can degrade activity over time. Proper labeling with batch number, activity, and expiry date is essential. Store in a cool, dry place. |
Technical Specifications
| CAS Number | 9001-73-4 |
| Solubility | Soluble in water; insoluble in most organic solvents |
| Storage Conditions | Store cool (2–8 °C), dry, sealed, protect from light |
| Shelf Life | 24 Months |
Applications & Usage
Common Applications:
meat tenderizing
protein hydrolysis
digestive supplements
wound debridement
cosmetics
Mechanism of action:
| Parameter | Papain |
|---|---|
| Functional Category | Enzyme Preparation; Meat Tenderizer; Dough Conditioner; Beverage Clarifying Agent. |
| Key Ingredients | Papain (a cysteine protease enzyme extracted from papaya latex, Carica papaya). |
| Mechanism of Action | Catalyzes the hydrolysis of peptide bonds within protein molecules, effectively breaking down large proteins into smaller peptides and amino acids. It has broad specificity, cleaving bonds adjacent to various amino acid residues, particularly targeting myofibrillar proteins (actin, myosin) and connective tissue proteins (collagen, elastin). |
| Application Effect in Product | Increases tenderness and reduces toughness in meat by degrading muscle fibers and connective tissue. Improves dough machinability and extensibility by weakening the gluten network. Prevents chill haze in beer and wine by hydrolyzing haze-forming polypeptides into soluble components. Enhances flavor profiles by releasing savory peptides and amino acids. |
Comparison:
| Product Name | Category/Type | Key Features | Strengths (vs peers) | Weaknesses (vs peers) | Best Use Cases | Why Choose |
|---|---|---|---|---|---|---|
| Papain | Cysteine Protease (Plant-derived) | Derived from papaya latex; broad specificity; active over a wide pH range (3-9); high thermostability. | Very robust in terms of temperature and pH tolerance. Widely available and cost-effective. | Can impart a slight flavor in sensitive food applications. Less specific cleavage than trypsin. | Meat tenderizing, beer chill-proofing, digestive supplements, wound debridement, cell isolation. | For general-purpose proteolysis requiring high heat stability and a broad effective pH range. |
| Bromelain | Cysteine Protease (Plant-derived) | Derived from pineapple stem/fruit; mixture of proteases; exhibits anti-inflammatory properties. | Dual function as a digestive aid and anti-inflammatory agent. Effective in both acid and alkaline environments. | Generally less thermostable than papain. Potency can vary between sources. | Dietary supplements (inflammation/digestion), meat tenderizing, food processing. | When anti-inflammatory properties are desired in addition to protein digestion, especially in supplements. |
| Ficin (Ficain) | Cysteine Protease (Plant-derived) | Derived from fig tree latex; very high proteolytic activity, especially on collagen. | Extremely high activity on certain substrates; effective milk coagulant. | Less commercially available and often more expensive. Can be a more potent allergen. | Cheese manufacturing (rennet substitute), gelatin production, laboratory diagnostics. | For specialized applications needing very potent activity, particularly against collagen or for milk coagulation. |
| Trypsin | Serine Protease (Animal-derived) | Derived from animal pancreas; highly specific cleavage at lysine and arginine residues; optimal pH ~8. | High specificity allows for precise, predictable protein cleavage. Well-characterized for lab use. | Animal source is unsuitable for vegan or certain religious applications. Narrow, alkaline optimal pH range. | Cell culture dissociation, proteomics, protein sequencing, pharmaceutical production. | For high-precision scientific or biotech work where cleaving proteins at specific sites is critical. |
| Actinidin | Cysteine Protease (Plant-derived) | Derived from kiwifruit; highly effective on muscle proteins (myosin, actin). | Superior meat tenderizing performance compared to papain. More neutral flavor profile. | Less heat stable than papain. Lower commercial availability and generally higher cost. | Premium meat tenderizing marinades, digestive aids focused on meat protein digestion. | When maximum meat tenderization with a neutral flavor is the primary goal. |
Technical Documents
Available Documentation
Spec Sheet, CoA, MSDS available
Safety Data Sheet (SDS)
MSDS available
Certificate of Analysis (COA)
Quality assurance documentation
Technical Data Sheet
Detailed technical specifications