Studies on lipase. IV. Purification and properties of a lipase secreted by Rhizopus delemer

  • FUKUMOTO JUICHIRO
    Osaka Municipal Technical Research Institute Also Laboratory of Enzyme Chemistry, Faculty of Science, Osaka City University
  • IWAI MIEKO
    Osaka Municipal Technical Research Institute
  • TSUJISAKA YOSHIO
    Osaka Municipal Technical Research Institute

書誌事項

タイトル別名
  • STUDIES ON LIPASE
  • Purification and properties of a lipase secreted by Rhizopus delemar
  • Studies of lipase. IV. Purification and properties of a lipase secreted by Rhizopus delemar
  • Studies on lipase IV. Purification and properties of a lipase secreted by Rhizopus delemar
  • IV. PURIFICATION AND PROPERTIES OF A LIPASE SECRETED BY <i>RHIZOPUS DELEMAR</i>

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説明

The purification of Rhizopus delemar lipase was undertaken to compare its enzymatic properties with those of the crystalline Aspergillus niger lipase (1). From culture filtrate of Rhizopus delemar grown by shaking culture, the enzyme was purified by ammonium sulfate fractionation, Duolite A2 resin treatment, SE-Sephadex column chromatography, acetone fractionation and gel-filtration by Sephadex G-75.<br>The specific activity of purified enzyme thus obtained was 2, 600-fold higher than that of the starting culture filtrate. Olive oil hydrolyzing activity of the enzyme was maximum at pH 5.6 and at 35°. The enzyme was stable at the range of pH 4 to 7 and at temperatures lower than 45°, but quickly inactivated above 50°. A weak esterase activity found in the enzyme preparation would be considered to be shown by the activity of the lipase itself.<br>Remarkable differences of the enzymatic properties of Rhizopus and Aspergillus lipases are found in their isoelectric points, turnover numbers and reaction conditions.

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