Proteolytic

Serratiopeptidase

A serine endopeptidase known for its ability to break down fibrin and other non-living protein matter in tissues. Its selectivity allows it to target protein-based waste products while leaving vital structural proteins largely unaffected, promoting efficient clearance of proteinaceous material.*

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ENZYME CLASSIFICATION

EC NUMBER | CAS NUMBER:
3.4.24.40 | 37312-62-2
ENZYME CLASS:
Hydrolase → Metalloprotease
ENZYME TYPE:
Systemic protease
ENZYME SOURCE:
Serratia marcescens
Enzyme Applications:
Dietary Supplements

TECHNICAL SPECIFICATIONS

ACTIVITY MEASUREMENT:
SPU (Serratiopeptidase Units)
PRIMARY SUBSTRATE:
Fibrin, denatured proteins, non-vital protein deposits
BOND CLEAVED:
Internal peptide bonds
PRIMARY PRODUCTS:
Peptides, amino acids
INACTIVATION:
55°C for 15 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.
Serratiopeptidase
Serratiopeptidase

BIOCHEMICAL ROLE IN SYSTEMIC FUNCTION

Serratiopeptidase hydrolyzes fibrin, inflammatory mediators, and certain proteinaceous secretions within tissues and circulation. By cleaving peptide bonds in insoluble protein aggregates, it contributes to remodeling processes that maintain tissue fluidity and structural balance. Its affinity for non-nutritive protein substrates, such as fibrin deposits, makes it a unique systemic protease compared to standard digestive proteases.*

NUTRITIONAL RELEVANCE IN SUPPLEMENTATION

Supplemental serratiopeptidase is often applied in systemic enzyme formulations to support vascular health, promote balanced inflammatory responses, and enhance recovery from tissue stress. Its fibrinolytic action is of particular interest in circulatory support, as it helps reduce the persistence of insoluble proteins that can accumulate during inflammatory or repair processes.*