Purification and Characterization of a Thermostable Lipase from Newly Isolated Pseudomonas sp. KWI-56(Microbiology & Fermentation Industry)
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概要
- 論文の詳細を見る
Newly isolated Pseudomonas sp. KWI-56 produced an extracellular thermostable lipase. The enzyme was purified 13.9-fold by acetone precipitation and gel filtration by HPLC with 2.9 % recovery. The purified enzyme, which showed a single band on SDS-PAGE, had a molecular weight of 33,000. The thermostability was very high, such that more than 96% of initial activity remained after incubation at 60℃ for 24 hr. The optimum temperature was 60℃ and the maximum hydrolysis of beef tallow reached 95 % at the reaction temperature of 50℃.
- 社団法人日本農芸化学会の論文
- 1990-05-23
著者
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Nagao Koji
Department Of Applied Biological Sciences Saga University
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Nakamura K
National Institute Of Bioscience And Human Technology
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Iizumi Taro
Kurita Central Laboratories, Kurita Water Industries Ltd.
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Nakamura Koichi
Kurita Central Laboratories, Kurita Water Industries Ltd.
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Fukase Tetsuro
Kurita Central Laboratories, Kurita Water Industries Ltd.
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Fukase T
Kurita Water Ind. Ltd. Atsugi‐shi Jpn
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Fukase Tetsuro
Kurita Central Laboratories Kurita Water Industries Ltd.
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Iizumi T
Kurita Water Ind. Ltd. Atsugi‐city Jpn
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Iizumi Taro
Kurita Central Laboratories Kurita Water Industries Ltd.
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Nakamura Koichi
Kurita Central Laboratories Kurita Water Industries Ltd
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NAKAMURA KAZUNORI
Kurita Central Laboratories, Kurita Water Industries Ltd.
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