title: Physiochemical properties of the native, zinc- and manganese-prepared metalloprotease of Bacillus polymyxa.
abstract: The neutral protease of Bacillus polymyxa had a broad pH optimum (6.0 to 7.2) for activity at 37 C. The enzyme was most stable at pH 5.6 to 5.8. The protease had an optimum temperature of 37 C and was quite thermostable up to 35 C, but at higher temperatures the stability decreased rapidly. The substrate specificity of the protease was similar to that of the neutral proteases of other members of the genus Bacillus. The enzyme was shown to be a zinc metalloprotease. However, manganous ions had a greater activating and stabilizing influence on the activity of this enzyme than zinc. Replacement of zinc in the native enzyme by manganese resulted in a 50% increase in activity. In addition, the prepared manganese metalloprotease had higher temperature and more alkaline pH optima than the native enzyme.
mesh_terms: D001059:Apoproteins / Q000032:analysis; D001407:Bacillus / Q000201:enzymology*; D002614:Chelating Agents / Q000494:pharmacology; D002854:Chromatography, Paper; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D008345:Manganese / Q000032:analysis; D008667:Metalloproteins; D008670:Metals / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000032:analysis / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D011480:Protease Inhibitors; D013054:Spectrophotometry, Atomic; D013696:Temperature; D015032:Zinc / Q000032:analysis*
chemical_list: D001059:Apoproteins; D002614:Chelating Agents; D008667:Metalloproteins; D008670:Metals; D010455:Peptides; D011480:Protease Inhibitors; D008345:Manganese; D010447:Peptide Hydrolases; D015032:Zinc