title: [Partial purification and properties of proteases of bitoxibacillin].
abstract: The paper describes properties of proteases A and B isolated from the biological insecticide bitoxibacillin by sulphate precipitation and Sephadex G-75 gel filtration. Proteases A and B of bitoxibacillin belong to the neutral bacterial proteases. pH optimum was found to be 6.0 and 7.5 for detection of proteolytic activity of protease A and protease B, respectively. Thermal stability of proteases A and B was similar and increased by 25% upon addition of CaCl2. Both proteases were inhibited with EDTA. The molecular weight of proteases A and B was estimated to be 57,000 and 47,000, respectively.
mesh_terms: D001413:Bacillus thuringiensis / Q000201:enzymology*; D007306:Insecticides; D007700:Kinetics; D008970:Molecular Weight; D009930:Organic Chemicals; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D007306:Insecticides; D009930:Organic Chemicals; C021633:Bitoxibacillin; D010447:Peptide Hydrolases
vernacular_title: Chastichnaia ochistka i svoĭstva proteaz preparata bitoksibatsillina.