Sharipova M R, Balaban N P, Nekhotyaeva N V, Mardanova A M, Dementiev A A, Leshchinskaya I B
Department of Microbiology, Kazan State University, Russian Federation.
Biochem Mol Biol Int. 1996 Apr;38(4):753-61.
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.
从产芽孢的中间芽孢杆菌的培养滤液中获得了一种新的碱性磷酸酶，并将其制备成了纯品。中间芽孢杆菌磷酸酶显示为分子量47 kDa的单体。该酶具有磷酸单酯酶和磷酸二酯酶活性，对多种底物表现出广泛的特异性。纯化后的磷酸酶最适温度为50℃，最适pH为9.5，在pH 8 - 10条件下，60℃时仍保持稳定。研究了二价金属离子和巯基试剂对该酶催化活性的影响。
