Purification and Characterization of an Esterase from <Emphasis Type="Italic">Acinetobacter lwoffii</Emphasis> I6C-1 |
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Authors: | Hye Eun Kim Kyeong Ryang Park |
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Institution: | (1) Dept. of Microbiology, Han Nam University, 133 Ojung-dong, Taeduk-ku, Taejon, 306-791 Korea, KR |
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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).
Received: 20 August 2001 / Accepted: 20 September 2001 |
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Keywords: | |
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