Merck, P3910-500MG, Protease from Bacillus licheniformis

General description
Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa.
Application
This is a proteolytic enzyme isolated from the fermentation of Bacillus licheniformis. It is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is for use in Total Dietary Fiber Assays (TDF-100A).
Biochem/physiol Actions
Subtilisin A is a member of the Serine S8 Endoproteinase family. It has broad specificity with a preference for a large uncharged residue in the P1 position. It hydrolyzes native and denatured proteins, and is active under alkaline conditions.
Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .
Other Notes
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per minute at pH 7.5 at 37°C.