Applied Microbiology and Biotechnology

, Volume 74, Issue 1, pp 107–112 | Cite as

Characterization of thermostable native alkaline phosphatase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1

  • Is Helianti
  • Takako Okubo
  • Yasutaka Morita
  • Eiichi TamiyaEmail author
Biotechnologically Relevant Enzymes and Proteins


This paper reports the characterization of an alkaline phosphatase (AP) from an aerobic hyperthermophilic Archaeon Aeropyrum pernix K1. The native AP was purified into homogeneity. The enzyme is predicted as a homodimeric structure with a native molecular mass of about 75 kDa and monomer of about 40 kDa. Apparent optimum pH and temperature were estimated at 10.0 and above 95°C, respectively. Magnesium ion increased both the stability and the activity of the enzyme. A. pernix AP has been demonstrated as a very thermostable AP, retaining about 76% of its activity after being incubated at 90°C for 5.5 h and 67% of its activity after being incubated at 100°C for 2.5 h, respectively, under the presence of Mg(II). Enzyme activity was increased in addition of exogenous Mg(II), Ca(II), Zn(II), and Co(II).


Hyperthermophilic Aeropyrum pernix Thermostable Alkaline phosphatase 


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Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • Is Helianti
    • 1
    • 2
  • Takako Okubo
    • 1
  • Yasutaka Morita
    • 1
    • 3
  • Eiichi Tamiya
    • 1
    Email author
  1. 1.School of Materials ScienceJapan Advanced Institute of Science and TechnologyIshikawaJapan
  2. 2.Center for Bioindustrial Technology (BPPT)JakartaIndonesia
  3. 3.Department of Biological and Environmental Chemistry, School of Humanity-Oriented Science and EngineeringKinki UniversityFukuokaJapan

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