Protease from Bacillus licheniformis

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

The enzyme is found to be stable at pH 8-10, retaining activity of up to 90% for 24 hours. It shows maximum activity at temperatures between 55-60 °C.

The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determination. It has also been used in the process of isolation of subsarcolemmal (SS) and intermyofibrillar (IMF) mitochondria that can be used for functional in vitro studies.

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.

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. Protease, Product P5380, is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane.

One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).