Proteolytic

Peptidase

An exopeptidase, catalyzes the stepwise removal of single amino acids from the ends of peptide chains. This final stage of protein digestion ensures that amino acids are fully liberated from dietary proteins and peptides, making them available for absorption into the bloodstream.*

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ENZYME CLASSIFICATION

EC NUMBER | CAS NUMBER:
3.4.11.1 | 9001-61-0
ENZYME CLASS:
Hydrolase → Peptidase
ENZYME TYPE:
Exopeptidase
ENZYME SOURCE:
Aspergillus oryzae
Enzyme Applications:
Dietary Supplements and Animal Nutrition

TECHNICAL SPECIFICATIONS

ACTIVITY MEASUREMENT:
HUT (Hemoglobin Unit Tyrosine)
PRIMARY SUBSTRATE:
Peptides and oligopeptides
BOND CLEAVED:
Terminal peptide bonds at the N- or C-terminus
PRIMARY PRODUCTS:
Free amino acids
INACTIVATION:
80°C for 30 minutes
FORM:
Powder
SOLUBILITY:
Water-soluble
STORAGE:
Store in a cool, dry environment
SHELF-LIFE:
18 months from MFG date if properly stored.
SAFETY & HANDLING:
Always refer to the included Safety Data Sheet.
Peptidase
Peptidase

BIOCHEMICAL ROLE IN DIGESTION

Peptidases (exo-acting amino- and carboxypeptidases) remove terminal residues from peptide chains generated by endoproteases, yielding free amino acids and small di-/tripeptides. This finishing step aligns with intestinal transport biology, as amino acids and select oligopeptides are the principal absorbable forms via dedicated transporters. Peptidases thus convert diverse peptide intermediates into forms that can rapidly transit the epithelium and enter systemic circulation.*

NUTRITIONAL RELEVANCE IN SUPPLEMENTATION

Supplemental peptidase ensures complete conversion of peptides to absorptive species, supporting efficient nitrogen utilization when brush-border activity is limited or protein intake is high. By reducing the pool of longer peptides that might persist into the colon, it helps maintain digestive comfort and nitrogen economy. In multi-enzyme formulations, peptidase provides the final relay, maximizing the nutritional yield of protein-containing foods.*