Protease from Bacillus licheniformis

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.

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).

Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .

Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa.

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.