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KMID : 1034820050010030189
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Molecular & Cellular Toxicology
2005 Volume.1 No. 3 p.189 ~ p.195
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Purification and Characterization of the Lipase from Acinetobacter sp. B2
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Sohn Sung-Hwa
Park Kyeong-Ryang
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Abstract
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Industrial development has increase consumption of crude oil and environmental pollution. A large number of microbial lipolytic enzymes have been identified and characterized to date. To development for a new lipase with catalytic activity in degradation of crude oil as a microbial enzyme, Acinetobactor sp. B2 was isolated from soil samples that were contaminated with oil in Daejon area. Acinetobactor sp. B2 showed high resistance up to 10 mg/mL unit to heavy metals such as Ba, Li, Al, Cr, Pb and Mn. Optimal growth condition of Acinetobactor sp. B2 was confirmed . Lipase was purified from the supernatant by Acinetobactor sp. B2. Its molecular mass was determined to the 60 kDa and the optimal activity was shown at and pH 10. The activation energies for the hydrolysis of p-nitrophenyl palmitate were determined to be 2.7 kcal/mol in the temperature range 4 to . The enzyme was unstable at temperatures higher than . The Michaelis constant for p-nitrophenyl palmitate were , respectively. The enzyme was strongly inhibited by , 2-Mercaptoethalol. From these results, we suggested that lipase purified from Acinetobactor sp. B2 should be able to be used as a new enzyme for degradation of crude oil, one of the environmental contaminants.
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KEYWORD
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lipase, Acinetobactor sp. B2, purification
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