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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.

참고문헌 (18)

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이 논문을 인용한 문헌 (4)

  1. 2006. "" Journal of microbiology and biotechnology, 16(11): 1832~1836 
  2. 2006. "" Journal of microbiology and biotechnology, 16(8): 1201~1209 
  3. Cho, Jaie-Soon 2009. "General Properties of Phytase Produced by Fluorescent Pseudomonas sp. BUN1" 한국동물자원과학회지 = Journal of animal science and technology, 51(2): 171~176 
  4. 2009. "" Journal of microbiology and biotechnology, 19(10): 1085~1091 


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