Purification and Characterization of Lipases from <i>Aspergillus repens</i> and <i>Eurotium herbariorum</i> NU-2 Used in &ldquo;<i>Katsuobushi</i>&rdquo; Molding

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  • Kaminishi Yoshio
    Department of Food Science and Technology, National Fisheries University
  • Tanie Hidetaka
    Department of Food Science and Technology, National Fisheries University
  • Kunimoto Masahiko
    Department of Food Science and Technology, National Fisheries University

書誌事項

タイトル別名
  • Purification and Characterization of Lipases from <i>Aspergillus repens</i> and <i>Eurotium herbariorum</i> NU-2 Used in “<i>Katsuobushi</i>” Molding
  • Purification and characterization of lipases from Aspergillus repens and Eurotium herbariorum NU-2 used in “Katsuobushi” molding

説明

Lipases (triacylglycerol acylhydrolase, EC 3. 1. 1. 3) were purified from Aspergillus repens and Eurotium herbariorum NU-2 strain by using a DEAE-Sephadex A-50 column and preparative electrophoresis. The purified enzymes from A. repens and NU-2 had molecular weights estimated by SDS-PAGE to be 38, 000 and 65, 000, respectively. Lipase from A. repens had a pH optimum of 5.3 and a temperature optimum of 27°C, while for the NU-2 strain corresponding values were pH 5.2 and 37°C. The specific activity of NU-2 was about twice that of A. repens. Substrate specificity toward olive oil or triolein and positional specificity for hydrolyzing the 1 (3)-position ester bonds of triacylglycerol are discussed for both enzymes.

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