Alkaline Protease (Bacillus subtilis)
Enzyme Preparations
Flavoring Agents
9014-01-1
$4.27 ~ $6.40
Food
Free sample from 100g(NF)
One unit of:25kg/barrel
One unit of:25kg/barrel
25kg/barrel
Product Info
What is Alkaline Protease (Bacillus subtilis)?
Alkaline Protease (Bacillus subtilis) is an industrial enzyme derived from the bacterium *Bacillus subtilis* that specifically hydrolyzes proteins in alkaline environments, primarily used in detergent manufacturing and various food processing applications.
How is Alkaline Protease (Bacillus subtilis) made?
| Step No. | Production Stage | Key Action | Control Point & Note |
|---|---|---|---|
| 1 | Inoculum Development | Select a high-yield strain of Bacillus subtilis and cultivate it in a sterile seed culture medium (shake flask or seed fermenter). | Strain purity is paramount. Aseptic techniques must be strictly followed to prevent contamination. Monitor growth parameters like cell density and pH. |
| 2 | Submerged Fermentation | Transfer the seed culture to a large, sterilized production fermenter containing a nutrient-rich medium. Induce enzyme production through controlled aeration and agitation. | Maintain optimal fermentation conditions: pH (alkaline, typically 9-11), Temperature (30-40°C), and Dissolved Oxygen (DO). This is the core stage where the enzyme is secreted by the bacteria. |
| 3 | Primary Recovery (Harvesting) | Separate the microbial cells and insoluble materials from the enzyme-rich fermentation broth, typically using centrifugation or microfiltration. | Ensure efficient separation to maximize the yield of the clarified, enzyme-containing liquid (supernatant). Minimize cell lysis to prevent release of intracellular contaminants. |
| 4 | Concentration & Purification | Concentrate the clarified broth to increase enzyme potency using ultrafiltration, which removes water and small molecule impurities. | Select a membrane with the appropriate Molecular Weight Cut-Off (MWCO) to retain the protease enzyme. Control temperature to prevent thermal denaturation. |
| 5 | Standardization & Formulation | Mix the concentrated enzyme with stabilizing agents (e.g., salts, sugars) and diluents to achieve a precise, standardized enzyme activity level. | Perform accurate enzyme activity assays (e.g., Casein Digestion Unit assay). Ensure thorough and uniform mixing for consistent product potency in every batch. |
| 6 | Drying (for solid forms) | Convert the liquid enzyme formulation into a stable powder or granule using methods like spray drying or fluid bed granulation. | Strictly control inlet and outlet temperatures during drying to avoid thermal inactivation of the enzyme. Monitor final moisture content and particle size for product stability. |
| 7 | Final QC & Packaging | Conduct final quality control tests on the finished product, verifying enzyme activity, microbial purity, moisture content, and physical form. Package into sealed, moisture-proof containers. | The final product must meet all pre-defined specifications. Proper packaging is critical to protect the enzyme from moisture, which can lead to activity loss. Ensure full traceability with batch codes. |
Technical Specifications
| CAS Number | 9014-01-1 |
| Solubility | Soluble in water; insoluble in organic solvents |
| Storage Conditions | Cool, dry, sealed place (≤25 °C), avoid moisture |
| Shelf Life | 12 Months |
Applications & Usage
Common Applications:
detergent
leather
baking
protein hydrolysates
silk degumming
Mechanism of action:
| Parameter | Alkaline Protease (Bacillus subtilis) |
|---|---|
| Functional Category | Enzymatic Tenderizer; Protein Modifier; Dough Conditioner; Flavor Developer |
| Key Ingredients | Alkaline protease enzyme derived from Bacillus subtilis fermentation; typically standardized with carriers like maltodextrin or salt. |
| Mechanism of Action | Catalyzes the hydrolysis of peptide bonds within protein molecules, primarily targeting myofibrillar (actin, myosin) and connective tissue (collagen, elastin) proteins. The enzyme's high activity at alkaline pH breaks down large protein structures into smaller, more soluble peptides and amino acids. |
| Application Effect in Product | Improved tenderness and texture in meat and poultry; enhanced dough extensibility and reduced mixing time in baking; increased protein solubility for beverage clarity; accelerated flavor development in protein hydrolysates and cheese ripening. |
Comparison:
| Product Name | Category/Type | Key Features | Strengths (vs peers) | Weaknesses (vs peers) | Best Use Cases | Why Choose |
|---|---|---|---|---|---|---|
| Alkaline Protease (Bacillus subtilis) | Bacterial Serine Protease | High activity at alkaline pH (8-12); broad substrate specificity; produced by fermentation. | Highly cost-effective; robust and stable in detergent formulations; well-established, high-yield production. | Lower thermostability compared to proteases from thermophilic organisms like B. licheniformis. | Laundry and dishwashing detergents, leather processing (dehairing), food protein hydrolysis, waste treatment. | A reliable, economical industry standard for general-purpose protein degradation in alkaline environments. |
| Alkaline Protease (Bacillus licheniformis) | Bacterial Serine Protease | Excellent thermostability; active at high alkaline pH (9-12); broad substrate specificity. | Superior heat tolerance allows for use in hot-wash cycles and high-temperature industrial processes. | Production can be slightly more expensive; performance can be very similar to B. subtilis protease at lower temperatures. | High-temperature detergents, animal feed additives, textile processing, industrial cleaning. | For applications requiring high performance and stability in hot, alkaline conditions. |
| Alkaline Protease (Aspergillus oryzae) | Fungal Serine Protease | Fungal origin; optimal pH range is often neutral to moderately alkaline; distinct substrate specificity. | Unique proteolytic action valuable in food processing for flavor development; avoids bacterial sources if required. | Generally less thermostable and has a narrower effective pH range than Bacillus proteases. | Food industry (baking, brewing, meat tenderizing, soy sauce fermentation), specialty chemical synthesis. | When a non-bacterial source is preferred or for specific food modification tasks. |
| Subtilisin Carlsberg | Bacterial Serine Protease (Endopeptidase) | A specific, highly-characterized enzyme from B. licheniformis; very broad substrate specificity. | Extremely active and effective for general protein removal; a benchmark enzyme with extensive research data. | Broad, non-specific action can be undesirable if controlled hydrolysis is needed; can be more expensive than crude preparations. | Detergents, contact lens cleaning solutions, laboratory research, biotransformations. | For applications needing a well-defined, highly active protease for non-specific protein digestion. |
| Trypsin | Animal-derived Serine Protease | Highly specific cleavage at the carboxyl side of lysine and arginine residues; optimal pH ~8.0. | Predictable and specific cleavage action, critical for analytical and biotech applications. | Very high cost; animal source raises concerns of variability and viral safety; less stable in harsh industrial conditions. | Cell culture (cell detachment), proteomics (mass spectrometry), insulin manufacturing, pharmaceutical processing. | For high-precision scientific or pharmaceutical work where specific peptide bond cleavage is essential. |
Technical Documents
Available Documentation
Specification sheet, CoA, MSDS available
Safety Data Sheet (SDS)
Available
Certificate of Analysis (COA)
Quality assurance documentation
Technical Data Sheet
Detailed technical specifications