小豆リポキシゲナーゼの部分精製と反応産物特異性
書誌事項
- タイトル別名
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- Partial purification and product specificity of adzukibean lipoxygenase.
抄録
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.
収録刊行物
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- 日本食品工業学会誌
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日本食品工業学会誌 38 (3), 214-216, 1991
社団法人 日本食品科学工学会
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詳細情報 詳細情報について
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- CRID
- 1390282681382624000
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- NII論文ID
- 130003788918
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- ISSN
- 00290394
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可