Not available outside of the UK & Ireland.

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

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

Packaging

500 mg in poly bottle

Physical properties

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

Specificity

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.

Unit Definition

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.