Description

• Specificity: A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.
• Application: Protease from Streptomyces griseus has been used:for the digestion of nucleus pulposus (NP) tissue[1]in the catalysis of asymmetric one pot Mannich reaction[2]for deproteinization of starch[3]digestion of brain slices for the cell dissociation[4]
• 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. Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. Serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.
• Features and Benefits: highly stable in pH range of 5.0 to 9.0, with peak activity at pH 8.8compatible with many DNA and RNA isolation buffersbroad substrate specificity
• Quality: Contains calcium acetate.
• Physical properties: Completely inactivated by heating above 80 °C for 15-20 minutes.
• Unit Definition: 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).
• Preparation Note: Collected from culture broth of S. griseus.