Isolation and partial characterization of a thermostable extracellular protease of Bacillus polymyxa B-17.
Bacillus polymyxa B-17, a sporeforming psychrotroph produced a thermostable protease. The protease was purified to homogeneity from cell free broth culture by precipitation with ammonium sulfate and gel filtration through Sephadex G-100. The enzyme had a temperature optimum at 50 degrees C and shared significant activity at 70 degrees C. The protease was also active over a wide range of pH, 5.5 to 10.0, and had optimum activity at pH 7.5. It was inhibited by metal chelating agents and has a molecular weight of 30 kDa.
Matta
H
H
Department of Microbiology, College of Basic Sciences, Himachal Pradesh Agricultural University, Palampur, India.
Punj
V
V
D000818:Animals; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002614:Chelating Agents / Q000494:pharmacology; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008892:Milk / Q000382:microbiology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D011480:Protease Inhibitors / Q000494:pharmacology
D001426:Bacterial Proteins; D002614:Chelating Agents; D011480:Protease Inhibitors; D010447:Peptide Hydrolases