[논문]Purification and Characterization of a Novel Extracellular Alkaline Phytase from Aeromonas sp.

SEO MYUNG-JI; KIM JEONG-NYEO; CHO EUN-AH; PARK HOON; CHOI HAK-JONG; PYUN YU-RYANG

Purification and Characterization of a Novel Extracellular Alkaline Phytase from Aeromonas sp. 원문보기

Journal of microbiology and biotechnology, v.15 no.4, 2005년, pp.745 - 748

SEO MYUNG-JI (Bioproducts Research Center Yonsei University) , KIM JEONG-NYEO (Department of Biotechnology, Yonsei University) , CHO EUN-AH (Department of Biotechnology, Yonsei University) , PARK HOON (Division of Applied Biological Sciences, Sunmoon University) , CHOI HAK-JONG (Gwen Knapp Center for Lupus and Immunology Research, Committee on Immunology and Department of Pathology, University of Chicago) , PYUN YU-RYANG (Department of Biotechnology, Yonsei University)

Abstract ▼ AI-Helper

A phytase from Aeromonas sp. LIK 1-5 was partially purified by ammonium sulfate precipitation and DEAE-Sephacel column chromatography. Its molecular weight was 44 kDa according to SDS-PAGE gel. Enzyme activity was optimal at pH 7 and at $50^{\circ}C$. The purified enzyme was strongly inhibited by 2 mM EDTA, $Zn^{2+},\;Co^{2+},\;or\;Mn^{2+}$, and activated by 2 mM $Ca^{2+}$. The K_m value for sodium phytate was 0.23 mM, and the enzyme was resistant to trypsin. The N-terminal amino acid sequence of the phytase was similar to that of other known alkaline phytases. The phytase was specific for ATP and sodium phytate, which is different from other known alkaline phytases. Based on the substrate specificity, the phytase may therefore be a novel alkaline phytase.

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