Subtilisin Carlsberg

Subtilisin Carlsberg is a well-studied bacterial serine protease and a member of the subtilase (serine protease) family S8, known for its broad substrate specificity and high activity at alkaline pH[3][1][8][2][4]. It is secreted by certain Bacillus species, notably Bacillus licheniformis and Bacillus subtilis, as a 275-amino acid globular protein that uses a classic serine protease catalytic triad (Asp-32, His-64, Ser-221) for hydrolysis of peptide bonds[6][5][1]. Its primary biological role is nutrient acquisition for bacteria via extracellular protein degradation, and it is extensively utilized as an industrial enzyme (for example, in laundry detergents, leather processing, and food industry)[2][3]. Subtilisin Carlsberg is not a biomolecular therapeutic target in humans or animals, nor is it a receptor, transporter, or disease-associated biomolecule; thus, it is not targeted by drugs, and it is not used for diagnostic or therapeutic biomarker purposes.

Other names

SubtilisinSubtilisin S41Serine endopeptidase CarlsbergBacillus subtilisin Carlsberg

Hydrolysis of peptide bonds via serine protease catalytic triad (Asp-His-Ser)