Protease from Streptomyces sp.

Pronase E can be used to degrade antheraea pernyi silk fibroin films.

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.

Completely inactivated by heating above 80 °C for 15-20 minutes.

Protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mM EDTA.

This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Proteases from Streptomyces griseus and Streptomyces omiyaensis have been used in a study to identify residue 71 as a crucial residue for differences in topological specificities. Proteases have also been used in a study to investigate production of protease as a by-product of streptomycin production.

Alkaline protease that is approximately twice as active at pH 11.0 than at the usual assay conditions for protease, pH 7.5 and 37 °C. By comparison, P5147 Type XIV protease is only approximately 25% as active at pH 11.0, 30 °C.

Isoelectric point : 8.7
Inhibitors : Diisopropyl fluorophosphate, EDTA
Optimum pH : >=12
Optimum temperature : 60^oC
pH Stability : pH 5.0 - 11.5 (25^oC,24hr)
Thermal stability : below 50^oC (pH 8.3, 15min)

One unit will hydrolyze casein to produce peptide equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 11.0 at 30 °C.

This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein.

Collected from culture broth of S.Sp