Studies on the Lipoprotein Lipases of Microorganisms

DOI
  • SAIKI Takashi
    Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
  • TAKAGI Yoshimasa
    Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo Amano Pharmaceutical Co. Ltd.
  • SUZUKI Teruji
    Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo Amano Pharmaceutical Co. Ltd.
  • NARASAKI Teiichi
    Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo Department of Agricultural Chemistry, Faculty of Agriculture, Kagawa University
  • TAMURA Gakuzo
    Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
  • ARIMA Kei
    Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo

Bibliographic Information

Other Title
  • Part IV Purification and General Properties of the Lipoprotein Lipase Produced by <i>Mucor javanicus</i>

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Description

Mucor javanicus IAM 6108 was cultivated aerobically at large scale in the medium containing corn steep liquor 3.0%, soluble starch 1.0%, soybean yuto 1.0% and inorganic salts, and the lipoprotein lipase produced was recovered by addition of ammonium sulfate (0.7 saturation). From this crude preparation, the enzyme was purified about 13times, through ammonium sulfate fractionation (0_??_0.4 saturation), precipitation at pH 4.0, ethanol precipitation (80%) and Sephadex G-200 gel filtration. The purified lipoprotein lipase was sedimented as single peak in ultracentrifugal analysis in the presence of 1.0% sodium dodecylsulfate. The enzymatic properties of the purified enzyme was as follows; optimum pH was 7.0, stable pH range was from 5.0 to 7.0, optimum temperature was 40°C, inactivated rapidly above 50°C. The lipoprotein lipase activity was inhibited by 75% and 88% by 10-2M taurocholate and 1.0M NaCl, respectively. ZnCl2, CuCl2, Pb(NO3)2, and SnCl2 at 10-3M showed complete inhibition. The ratio of lipoprotein lipase to lipase activity was 10:1. Lipoprotein lipase activity was dependent on the concentration of blood plasma which could be substituted by bovine serum albumin or egg albumin to a certain degree. The results suggesting the preferential α-fatty acid hydrolysis was obtained.

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Details 詳細情報について

  • CRID
    1390282681444190976
  • NII Article ID
    130003415408
  • DOI
    10.1271/bbb1961.33.414
  • COI
    1:CAS:528:DyaF1MXkt1Omsbg%3D
  • ISSN
    18811280
    00021369
  • Text Lang
    en
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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