Partial purification and product specificity of adzukibean lipoxygenase.

DOI
  • YAMAMOTO Aijiro
    Department of Nutrition, College of Nutrition, Koshien University
  • YAMADA Kazue
    Department of Nutrition, College of Nutrition, Koshien University
  • HAYASHI Chieko
    Department of Nutrition, College of Nutrition, Koshien University
  • TANIDA Naoko
    Department of Nutrition, College of Nutrition, Koshien University

Bibliographic Information

Other Title
  • 小豆リポキシゲナーゼの部分精製と反応産物特異性

Abstract

Lipoxygenase (EC 1. 13. 11. 12) from adzukibeans was partially purified and some characteristics were examined to understand the mechanism by which the stale cooked flavor was formed in stored adzukibeans. The adzukibean enzyme specifically acted on the free form of polyunsaturated fatty acids and was more labile than soybean enzyme (L-1 type). Incubation of linoleic acid with this enzyme yielded 13- to 9- hydroperoxides at a ratio of 48:52. The adzukibean enzyme, which has the optimum pH around 6.5 and is activated by calcium ion, is different from soybean (L-1 type) and rice germ enzymes in the composition of hydroperoxide isomers formed, and similar to the soybean isozyme (L-2 type), which is reported to play a main role in the development of n-hexanal in soybean flavors.

Journal

Details 詳細情報について

  • CRID
    1390282681382624000
  • NII Article ID
    130003788918
  • DOI
    10.3136/nskkk1962.38.214
  • ISSN
    00290394
  • Text Lang
    ja
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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