Purification and Characterization of a Lipase from Aspergillus oryzae

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概要

• 論文の詳細を見る

• A lipase from Aspergillus oryzae was purified by ammonium sulfate fractionation, anion exchange chromatography, hydrophobic interaction chromatography, and anion exchange chromatography. The purified enzyme was a monomeric protein with a molecular mass of 41 kDa estimated by SDS-PAGE and 39 kDa by gel filtration. The optimum pH at 30℃ and optimum temperature at pH 7.0 were 7.0 and 30℃, respectively. The enzyme was stable over a pH range of 6-9 at 25℃ for 18 h, and up to 30℃ at pH 7.0 for 3 h. Ag^+, Fe^<3+>, Hg^<2+>, Cu^<2+>, and Zn^<2+> inhibited the enzyme activity severely. The enzyme was a lipase that hydrolyzed monoacylglycerols and diacylglycerols, but did not hydrolyze triacylglycerols. The N-terminal amino acid sequence of the enzyme was highly homologous with that of the mono- and diacylglycerol lipase from Penicillium camembertii U-150.

• 社団法人日本農芸化学会の論文
• 1995-07-23

著者

• Kondoh Kimio

  Food Technology Research Institute Of Nagano Prefecture

• Ohnishi Kunio

  Research Institute Takeya Miso Co. Ltd.

• FUKUZAWA MIKIO

  Food Technology Research Institute of Nagano Prefecture

• TOIDA Jinichi

  Food Technology Research Institute of Nagano Prefecture

• Sekoguchi Junichi

  Department of Applied Biology, Faculty of.Textile Science and Technology, Shinshu University

• Sekoguchi Junichi

  Department Of Applied Biology Faculty Of.textile Science And Technology Shinshu University

関連論文

• Lipase Production of Aspergillus oryzae
• Isolation of Sake Yeast Mutants Producing a High Level of Ethyl Caproate and/or Isoamyl Acetate
• Purification and Characterization of a Novel Lipolytic Enzyme from Aspergillus oryzae
• Accumulation of a Recombinant Aspergillus oryzae Lipase Artificially Localized on the Bacillus subtilis Cell Surface
• Purification and Characterization of Triacylglycerol Lipase from Aspergillus oryzae
• Purification and Characterization of a Lipase from Aspergillus oryzae

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