in the catalysis of asymmetric one pot Mannich reaction
for deproteinization of starch
digestion of brain slices for the cell dissociation
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 8.8
compatible with many DNA and RNA isolation buffers
broad substrate specificity
Physical properties
Completely inactivated by heating above 80 °C for 15-20 minutes.
Preparation Note
Collected from culture broth of S. griseus.
Quality
Contains calcium acetate.
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.
Unit Definition
One unit will hydrolyze casein to produce color equivalent to 1.0
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