Description
Alkaline Protease (subtilisin, Bacillus serine endopeptidase) is a broad-specificity endopeptidase active at alkaline pH. In food processing it is the principal protease for high-degree-of-hydrolysis protein hydrolysates, the production of bioactive peptides, and alkaline meat-co-product recovery.
Off-white to light tan free-flowing powder, or amber liquid. Activity is standardised in Alkaline Protease Units defined by the Folin-Ciocalteu method on casein at pH 10.0.
We supply food-grade Alkaline Protease from manufacturers in China holding ISO 22000, Halal, Kosher and other certifications relevant to the product and production. Bacillus licheniformis and Bacillus subtilis are the dominant source organisms.
Common market grades include 100,000 U/g standard food grade, 200,000 to 400,000 U/g concentrated for protein-hydrolysate production, 600,000 U/g high-activity grade, and bioactive-peptide manufacture grades with defined peptide-bond cleavage profiles.
Bulk and reduced-MOQ shipments. Batch-level COA covering activity, pH optimum, temperature optimum, moisture, heavy metals and microbiology.
Introduction
Alkaline Protease, marketed historically as subtilisin or Alcalase, has been a workhorse industrial protease since the 1960s. The enzyme found early use in detergent formulations and reached food-industry scale in the 1980s with the rise of protein-hydrolysate and clinical-nutrition manufacture.
Industrial production is by submerged fermentation of selected Bacillus licheniformis and Bacillus subtilis strains. Modern preparations are tuned by strain selection and downstream blending to deliver the peptide-bond cleavage profile required for the target hydrolysate, with low-bitterness variants and bioactive-peptide-targeted variants available.
The enzyme is Generally Recognized as Safe by the U.S. FDA from approved Bacillus strains, listed in the JECFA enzyme compendium, and approved as a processing aid in the EU.
Mechanistically, subtilisin is a serine endopeptidase with the classical serine-histidine-aspartate catalytic triad. It hydrolyses internal peptide bonds with a broad specificity preferring hydrophobic and aromatic residues at the P1 position. The enzyme operates optimally at pH 8.0 to 10.0 and 55 to 65 degrees Celsius, and tolerates alkaline conditions that inactivate most other food proteases.
Strategic positioning is central to the global protein-hydrolysate industry: alkaline protease, neutral protease and acid protease together cover the full pH spectrum of industrial protein processing, with alkaline protease taking the high-degree-of-hydrolysis and bioactive-peptide segments where deep, broad cleavage is the goal.
Where it is used
- High-degree-of-hydrolysis protein hydrolysate manufacture from soy, whey, casein and pea proteins
- Bioactive peptide production; targeted hydrolysis for ACE-inhibitor and antioxidant peptide manufacture
- Collagen hydrolysate and gelatin peptide manufacture; defined molecular-weight collagen peptides
- Fish, krill and marine protein hydrolysate manufacture; alkaline-pH recovery of co-product proteins
- Yeast extract production; alkaline hydrolysis-stage proteolysis
- Casein and whey peptone production for microbiological media
- Animal feed; alkaline pre-digestion of plant and animal proteins
- Hide and bone protein recovery for collagen, gelatin and bone-broth ingredient manufacture
- Allergenicity reduction in selected protein hydrolysate products
Technical data
| Item | Specification |
|---|---|
| Appearance | Off-white to light tan powder or amber liquid |
| Activity | 100,000 to 600,000 U/g or per customer specification |
| pH optimum | 8.0 to 10.0 |
| Temperature optimum | 55 °C to 65 °C |
| Moisture (powder) | ≤ 8.0% |
| Heavy metals (as Pb) | ≤ 10 mg/kg |
| Arsenic | ≤ 3 mg/kg |
| Total plate count | ≤ 50,000 CFU/g |
| Coliforms | ≤ 30 CFU/g |
| Salmonella | Absent in 25 g |
| E. coli | Absent in 25 g |
| Source organism | Bacillus licheniformis or Bacillus subtilis |
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