Purification and Some Properties of Lipase Produced by Pseudomonas fragi 22.39 B(Biological Chemistry)
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概要
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The lipase (EC. 3.1.1.3) of Pseudomonas fragi 22.39 B was purified by acidification of the culture supernatant, ammonium sulfate fractionation, and column chromatography on DEAE-Toyopearl 650M and DEAE-Sepharose CL-6B. The recovery of activity was about 48%. The purified lipase was homogeneous electrophoretically and its molecular weight was 33,000. The optimum pH and temperature for hydrolysis of olive oil emulsion were 9.0 and 65℃, respectively. The enzyme was stable up to 51℃ at pH 9.0 for 24hr and in a pH range from 6.5 to 10.5 at 30℃ for 24hr. The lipase was inhibited by Zn^<2+>, Fe^<2+>, Fe^<3+> and cationic surfactants such as cetyltrimethyl-ammonium bromide.
- 社団法人日本農芸化学会の論文
- 1987-01-23
著者
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Nishio Toshiyuki
Research And Development Laboratories Sapporo Breweries Ltd.
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Nishio Toshiyuki
Research & Development Laboratories Sapporo Breweries Ltd.
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KAMIMURA Minoru
Research & Development Laboratories, Sapporo Breweries Ltd.
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CHIKANO Takahide
Research & Development Laboratories, Sapporo Breweries Ltd.
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Kamimura M
Brewing Research Laboratories Sapporo Breweries Ltd.
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Chikano Takahide
Research And Development Laboratories Sapporo Breweries Ltd.
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