A novel Bacillus intermedius extracellular alkaline phosphatase: isolation, physico-chemical and catalytic characteristics.
A new alkaline phosphatase was obtained as homogeneous preparation from culture filtrate of the spore-forming Bacillus intermedius. B. intermedius phosphatase was shown to be monomer with molecular weight of 47 kDa. The enzyme possesses phosphomonoesterase and phosphodiesterase activities and exhibits a broad specificity towards a wide variety of substrates. The purified phosphatase had an optimum temperature of 50 degrees C, optimum pH of 9.5 and was stable until 60 degrees C at pH 8-10. The effect of divalent metal ions and thiol reagents on catalytic activity of the enzyme was studied.
Sharipova
M R
MR
Department of Microbiology, Kazan State University, Russian Federation.
Balaban
N P
NP
Nekhotyaeva
N V
NV
Mardanova
A M
AM
Dementiev
A A
AA
Leshchinskaya
I B
IB
D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002852:Chromatography, Ion Exchange; D004586:Electrophoresis; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D000469:Alkaline Phosphatase