Dec 29, 1998

Isolation and properties of extracellular alkaline phosphatase from Bacillus intermedius

Biochemistry. Biokhimii︠a︡
M R SharipovaI B Leshchinskaya

Abstract

Alkaline phosphatase (APase) was isolated from the culture liquid of the streptomycin-resistant strain of Bacillus intermedius S3-19 and purified as a homogeneous preparation by ion-exchange chromatography and FPLC. Electrophoresis and gel-filtration revealed that the active enzyme is a monomer with molecular weight of 46-47 kD. The enzyme possessed phosphomonoesterase and phosphodiesterase activities with maximal levels at pH 9.5 and 55 degreesC and was stable until 60 degreesC at pH 8.0-10.0. The isolated APase exhibits a broad specificity towards a wide variety of substrates. The effect of divalent metal ions and other reagents on its catalytic activities was studied. It was concluded that alkaline phosphatase of B. intermedius is similar to the secreted alkaline phosphatases from other Bacillus species in its physicochemical and catalytic properties.

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Mentioned in this Paper

Cations, Divalent
Fast Protein Liquid Chromatography
Filtration
Phosphoric Monoester Hydrolases
Extracellular
Phosphoric diester hydrolase
Alkaline Phosphatase Measurement
Bacillus intermedius
Bacillus species
Alkaline Phosphatase

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