Purification and Some Properties of a Castor-oil-hydrolyzing Lipase from Pseudomonas sp.(Biological Chemistry)
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概要
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To obtain a lipase which effectively hydrolyzes castor oil, bacteria were isolated from 500 soil samples. The best strain was examined; its microbiological characteristics suggested that it belongs to the genus Pseudomonas. A lipase from this strain was purified by ammonium sulfate fractionation and chromatographies on DEAE-cellulose and DEAE-Toyopearl 650 M. The enzyme was purified about 400-fold with a yield of 13%. The purified enzyme was electrophoretically homogeneous and its molecular weight was 30,000. The optimum pH and temperature for the hydrolysis of olive oil emulsion were 7.0 and 60℃. The enzyme was stable up to 35℃ at pH 7.0 for 30 min and also stable from pH 9.0 to 10.0 at 4℃ for 22 hr. The activity was inhibited by Fe^<3+>, Hg^<2+>, pCMB, and anionic surfactants, and enhanced by nonionic surfactants and bile salts. The enzyme efficiently hydrolyzed castor oil.
- 社団法人日本農芸化学会の論文
- 1988-12-23
著者
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Fujiwara Nobuaki
Osaka Prefectural Industrial Research Institute
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YAMAMOTO KAZUHIKO
Osaka Prefectural Industrial Technology Research Institute
関連論文
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- Utilization of a Thermostable Alkaline Protease from an Alkalophilic Thermophile for the Recovery of Silver from Used X-Ray Film
- Purification and Some Properties of a Castor-oil-hydrolyzing Lipase from Pseudomonas sp.(Biological Chemistry)
- The Hydrolysis of Castor Oil Using a Lipase from Pseudomonas sp. f-B-24 : Positional and Substrate Specificity of the Enzyme and Optimum Reaction Conditions
- Production of Alkaline Protease in a Low-Cost Medium by Alkalophilic Bacilus sp. and Properties of the Enzyme