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KMID : 1094720000050010053
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Biotechnology and Bioprocess Engineering
2000 Volume.5 No. 1 p.53 ~ p.56
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Partial purification and characterization of thermostable esterase from the hyperthermophilic archaeonSulfolobus solfataricus
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Chung Young-Mi
Park Chan-B.
Lee Sun-Bok
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Abstract
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A thermostable esterase from the hyperthemophilic archaeonSulfolobus solfataricus was partially purified 590-fold with 16.2% recovery. The partially purified esterase had a specific activity of 29.5μmol min?1 mg?1 when the enzyme activity was determined usingp-nitrophenyl butyrate as a substrate. The apparent molecular weight was about 100 kDa, while the optimum temperature and pH for esterase were 75°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 thatS. solfataricus esterase can be used for the production of commercially important chiral drugs.
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KEYWORD
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S. solfataricus, thermostable esterase, ibuprofen resolution
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