Neutral Protease
Enzyme Preparations
9068-59-1
$7.99 ~ $11.98
Food
Free sample from 100g(NF)
One unit of:25kg/barrel
One unit of:25kg/barrel
25kg/barrel
Product Info
What is Neutral Protease?
Neutral Protease is an enzyme, often derived from *Bacillus subtilis*, that specifically hydrolyzes proteins under neutral pH conditions, primarily utilized in the food industry as a dough conditioner in baking and a clarifying agent in brewing.
How is Neutral Protease made?
| Step No. | Production Stage | Key Action | Control Point & Note |
|---|---|---|---|
| 1 | Seed Culture Preparation | Inoculate a sterile seed medium with a pure strain of the production microorganism (e.g., Bacillus subtilis) and incubate. | Control Points: Strain purity is paramount. Monitor temperature, pH, agitation, and incubation time. Strict aseptic techniques must be used to prevent contamination. |
| 2 | Fermentation | Transfer the seed culture to a large, sterile fermenter containing the production medium. Run the fermentation process under controlled conditions. | Control Points: Maintain optimal temperature (30-40°C), pH (6.5-7.5), dissolved oxygen (DO), and agitation. The process is monitored for enzyme activity yield until it reaches its peak. |
| 3 | Harvesting & Separation | Separate the enzyme-rich liquid broth from the microbial cells and other solid insolubles. | Control Points: Typically achieved via centrifugation or microfiltration. The efficiency of solid-liquid separation is key. The process is often chilled to maintain enzyme stability. |
| 4 | Purification & Concentration | Concentrate the clarified enzyme solution and remove low-molecular-weight impurities. | Control Points: Ultrafiltration (UF) is commonly used. The membrane's molecular weight cut-off (MWCO) is critical. Monitor pressure and temperature to prevent enzyme denaturation while maximizing concentration. |
| 5 | Standardization & Formulation | Adjust the enzyme concentrate to the desired activity level by adding stabilizers and diluents. | Control Points: Precise measurement of enzyme activity is required. Accurate blending with excipients (e.g., maltodextrin, salt) and stabilizers (e.g., calcium salts) ensures the final product meets activity specifications. |
| 6 | Drying | Convert the liquid enzyme formulation into a stable powder form. | Control Points: Spray drying is typical. Inlet and outlet air temperatures are strictly controlled. Temperatures must be low enough to prevent thermal deactivation of the enzyme. Final moisture content is a critical quality parameter. |
| 7 | Quality Control & Packaging | Blend the dried powder for uniformity, perform final quality analysis, and package the finished product. | Control Points: Test for final enzyme activity, moisture, particle size, and microbiological purity (e.g., total plate count, E. coli, Salmonella). Packaging must be in airtight, moisture-proof containers to ensure shelf life and stability. |
Technical Specifications
| CAS Number | 9068-59-1 |
| Solubility | Soluble in water |
| Storage Conditions | Store in a cool, dry place at 2–8 °C |
| Shelf Life | 24 Months |
Applications & Usage
Common Applications:
protein hydrolysate production
collagen extraction
baking
brewing
flavor enhancement
Mechanism of action:
| Parameter | Neutral Protease |
|---|---|
| Functional Category | Enzymatic Processing Aid; Tenderizer; Dough Conditioner; Flavor Modifier |
| Key Ingredients | Proteolytic enzyme (Neutral Protease) derived from microbial fermentation (e.g., Bacillus amyloliquefaciens or Aspergillus oryzae) |
| Mechanism of Action | Catalyzes the hydrolysis of internal peptide bonds within protein molecules (endopeptidase activity). It specifically targets peptide bonds involving hydrophobic amino acid residues, breaking down large, complex proteins (e.g., gluten, collagen, casein) into smaller, more soluble polypeptides and peptides. Optimal activity occurs at a neutral pH range (6.0-7.5). |
| Application Effect in Product | Increases tenderness and succulence in meat products by degrading myofibrillar and connective tissue proteins; reduces mixing time and improves dough extensibility/machinability in bakery applications (e.g., crackers, biscuits); enhances savory (umami) flavor notes in protein hydrolysates, sauces, and seasonings; clarifies beverages by precipitating haze-forming proteins. |
Comparison:
| Product Name | Category/Type | Key Features | Strengths (vs peers) | Weaknesses (vs peers) | Best Use Cases | Why Choose |
|---|---|---|---|---|---|---|
| Neutral Protease | Metalloendopeptidase | Optimal activity at neutral pH (6.5-7.5); often requires metal ions (e.g., Zn2+) for stability. | Gentle action under physiological conditions, minimizing damage to sensitive materials or unwanted side reactions. | Ineffective in highly acidic or alkaline environments; can be inhibited by chelating agents like EDTA. | Baking, brewing, leather softening, cell culture, contact lens cleaners where pH neutrality is key. | For processes requiring gentle protein modification at or near neutral pH, protecting delicate substrates. |
| Alkaline Protease | Serine endopeptidase | Optimal activity at alkaline pH (8-12); often thermostable. | Highly effective and stable in harsh, high-pH environments common in cleaning and industrial processing. | Can be too aggressive for sensitive proteins; inactive at neutral or acidic pH. | Laundry and dish detergents, de-hairing hides, industrial waste treatment, protein stain removal. | When maximum proteolytic power is needed in alkaline conditions, such as for cleaning applications. |
| Acid Protease | Aspartic endopeptidase | Optimal activity at acidic pH (2.5-5.0). | Functions effectively in low-pH conditions where most other proteases are denatured. | Inactive at neutral or alkaline pH; may have less substrate specificity than others. | Animal feed digestion aid, soy sauce fermentation, preventing beer haze, cheese making (rennet). | For applications that operate in a strongly acidic environment, like digestive aids or specific food fermentations. |
| Papain | Cysteine endopeptidase | Plant-derived (papaya); broad effective pH range (3-10); activated by reducing agents. | Extremely versatile across a wide pH spectrum; widely available and generally recognized as safe (GRAS) for food. | Activity can be inconsistent based on purity and source; requires specific activators and is sensitive to oxidation. | Meat tenderizing, beer chill-proofing, wound debridement, digestive supplements. | For a versatile, plant-based option that works well across various conditions, especially in food applications. |
| Trypsin | Serine endopeptidase | Animal-derived; highly specific cleavage site (after Lysine or Arginine); optimal pH 7.5-8.5. | Predictable and controlled protein digestion due to high specificity; prevents random degradation. | Narrow range of target proteins; animal origin can be an issue for some applications; easily inhibited. | Cell culture (detaching cells), proteomics and protein sequencing, insulin manufacturing, infant formula. | When precise, specific cleavage of proteins is required for analytical or biomedical purposes. |
Technical Documents
Available Documentation
Spec Sheet, MSDS available
Safety Data Sheet (SDS)
Available
Certificate of Analysis (COA)
Quality assurance documentation
Technical Data Sheet
Detailed technical specifications