書誌事項
- タイトル別名
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- Antioxidative Activity of Peptides Prepared by Enzymatic Hydrolysis of Egg-white Albumin.
- ラン アルブミン ノ コウソ ブンカイ ニ ヨッテ エラレル ペプチド ノ コ
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抄録
The antioxidative activity of protease hydrolyzates of four proteins against linoleic acid was investigated in an aqueous system at pH 7.0. Eight kinds of protease were used. The egg-white albumin hydrolyzate prepared with Amano S (from Bacillus subtilis) had the strongest antioxidative activity. From this hydrolyzate, three antioxidative peptides were purified by Sephadex G-25 gel filtration, CM Sephadex C-25 column chromatography, and then HPLC on an octadeceyl column. The amino acid sequences of the peptides were Ala-His-Lys (P 1), Val-His-His (P 2), and Val-His-His-Ala-Asn-Glu-Asn (P 3). The antioxidative activity of P 1 was the strongest, and the activities of P 2 and P 3 were about half that of P 1. A mixture of Fe2+ and egg-white albumin hydrolyzate was separated by Sephadex G-25 gel filtration, and the recovery of Fe2+ was measured. Most of the bound iron was eluted in the fractions corresponding to the peak of the antioxidative activity. This suggests that the antioxidative activity was based on the chelating activity of the peptides.
収録刊行物
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- 日本農芸化学会誌
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日本農芸化学会誌 65 (11), 1635-1641, 1991
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282679483463168
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- NII論文ID
- 130001228215
- 10011626904
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- NII書誌ID
- AN00196191
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- COI
- 1:CAS:528:DyaK38XlslKksQ%3D%3D
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- ISSN
- 18836844
- 00021407
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- NDL書誌ID
- 3747170
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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
- NDL
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- 抄録ライセンスフラグ
- 使用不可