Biotechnology and Bioprocess Engineering:BBE

  • 제5권1호
  • /
  • Pages.53-56
  • /
  • 2000
  • /
  • 1226-8372(pISSN)
  • /
  • 1976-3816(eISSN)
한국생물공학회 (The Korean Society for Biotechnology and Bioengineering)
권호 표지

Partial Purification and Characterization of Thermostable Esterase from the Hyperthermophilic Archaeon Sulfolobus solfataricus

  • Chung Young Mi (Department of Chemical Engineering, Pohang University of Science and Technology) ;
  • Park Chan B. (Department of Chemical Engineering, Pohang University of Science and Technology) ;
  • Lee Sun Bok (Department of Chemical Engineering, Pohang University of Science and Technology)
  • 발행 : 2000.01.01
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초록

A thermostable esterase from the hyper thermophilic archaeon Sulfolobus solfataricus was partially purified 590-fold with $16.2\%$ recovery. The partially purified esterase had a specific activity of $29.5\;{\mu}mol\;min^{-1}mg^{-1}$ when the enzyme activity was determined using p-nitrophenyl butyrate as a substrate. The apparent molecular weight was about 100 kDa, while the optimum temperature and pH for esterase were $75^{\circ}C$ and 8.0, respectively. The enzyme showed high thermal stability and solvent tolerance in comparison to its mesophilic counterpart. The enzyme also showed chiral resolution activity for (S)-ibuprofen, indicating that S. solfataricus esterase can be used for the production of commercially important chiral drugs.

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참고문헌

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