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Current Microbiology

, Volume 44, Issue 6, pp 401–405 | Cite as

Purification and Characterization of an Esterase from Acinetobacter lwoffii I6C-1

  • Hye Eun Kim
  • Kyeong Ryang Park
Article

Abstract

EstA was purified from the supernatant by A. lwoffii 16C-1. Its molecular mass was determined to be 45 kDa, and the optimal activity occurred when the pH level was 8.0 at a temperature of 37°C. The activation energies for the hydrolysis of p-nitrophenyl butyrate was determined to be 11.25 kcal/mol in the temperature range of 10–37°C. The enzyme was unstable at temperatures higher than 50°C. The Michaelis constant (K m ) and V max for p-nitrophenyl butyrate were 11 μM and 131.6 μM min−1 mg of protein-1, respectively. The enzyme was strongly inhibited by Hg2−, Ca2+, Mg2+, Fe2+, Cu2+, Zn2+, Mn2+, Co2+, ethylemediaminetetraacetic acid (EDTA), phenylmethylsulfonyl fluoride (PMSF), and diisopropyl fluorophosphate (DFP).

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Copyright information

© Springer-Verlag New York Inc. 2002

Authors and Affiliations

  • Hye Eun Kim
    • 1
  • Kyeong Ryang Park
    • 1
  1. 1.Dept. of Microbiology, Han Nam University, 133 Ojung-dong, Taeduk-ku, Taejon, 306-791 KoreaKorea

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