Protease

Proteases are a broad class of enzymes that catalyze the hydrolysis of peptide bonds, breaking down proteins into amino-acid fragments. In supplementation, protease blends, often derived from pancreatic, bacterial, or plant sources, are used primarily to support digestive protein breakdown and to modulate inflammatory pathways.

• Molecular Structure: Proteases are high-molecular-weight proteins (20–250 kDa) composed of amino-acid chains folded into a catalytic domain and, often, a regulatory domain.
• Catalytic Center: The catalytic center usually contains a serine-histidine-aspartate triad (e.g., trypsin: Asp-102, His-57, Ser-195) or a zinc-binding motif (HEXXH) in metalloproteases.
• Nomenclature: No single IUPAC name applies; instead, each enzyme is identified by its EC number (e.g., EC 3.4.21.4 for trypsin).
• Physicochemical Properties: Typical physicochemical properties: pH optimum 6.0–8.5 for pancreatic enzymes, 2–4 for gastric pepsin; temperature optimum 37–40 °C. Molecular weight and activity are expressed in units (U) or International Units (IU) per milligram of protein.

• Animal pancreas (porcine, bovine): Pancreatin extracted via aqueous extraction, followed by ultrafiltration and lyophilization.
• Microbial fermentation (Bacillus subtilis, Aspergillus oryzae): Recombinant expression in fermenters yields high-purity proteases (e.g., Bacillus lactamase-type protease).
• Plant sources: Bromelain (Ananas comosus) and papain (Carica papaya) obtained by aqueous extraction, followed by precipitation and spray-drying.
• Quality Control: Quality-control measures include activity assays (USP <231>), contaminant testing (viral, bacterial endotoxin), and verification of source-specific allergens. For therapeutic use, GMP-certified manufacturers must provide batch-specific enzyme activity, purity (>95 % protein), and stability data (shelf-life ≥ 24 months).