Biochemical Studies on Rice Bran Lipase

• FUNATSU Masaru

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• AIZONO Yasuo

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• HAYASHI Katsuya

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• WATANABE Masayoshi

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• ETO Masakazu

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

書誌事項

タイトル別名

• Part I. Purification and Physical Properties

抄録

Lipase extracted from defatted rice bran with calcium chloride solution was purified by ammonium sulfate precipitation, followed by successive column chromatographies on DEAE-cellulose, Sephadex G-75, CM-Sephadex C-50 in the presence of calcium ion. The specific activity of the purified enzyme was 4.7 units/mg protein and 480 times that of starting crude extract. The homogeneity of the enzyme protein was criticized by polyacrylamide gel disc electrophoresis and ultracentrifugation. The enzyme protein also behaved homogeneously in ampholine electrophoresis, indicating the isoelectric point of 8.56. The sedimentation coefficient of the enzyme was determined to be 2.97 S, and the molecular weight to be 40000 by Archibald's method. According to the measurement of optical rotatory dispersion of the enzyme, ORD constant, λ_c, Moffitt-Yang parameters, a₀ and b₀, were evaluated to be 239mμ, , -164 and -123, respectively.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 35 (5), 734-742, 1971

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390282681443051904
• NII論文ID: 130003523663
• DOI: 10.1271/bbb1961.35.734
• COI: 1:CAS:528:DyaE3MXkslWlsbo%3D
• ISSN: 18811280
• ISSN: 00021369
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可