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[Partial purification and properties of proteases of bitoxibacillin].

M Kuchera, Barbashova Nm

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.

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Available abstract

Key concepts: Proteases, Protease, Sephadex, Chemistry, Biochemistry, Size-exclusion chromatography, Enzyme, Chromatography