九州大学大学院生物資源環境科学研究科生物機能科学専攻食品バイオ工学講座
Laboratory of Food Analysis, Institute of Food Biotechnology, Department of Bioscience and Biotechnology, Division of Bioresource and Bioenvironmental Sciences, Graduate School Kyushu University
九州大学大学院生物資源環境科学研究科生物機能科学専攻食品バイオ工学講座
Laboratory of Food Analysis, Institute of Food Biotechnology, Department of Bioscience and Biotechnology, Division of Bioresource and Bioenvironmental Sciences, Graduate School Kyushu University
九州大学大学院生物資源環境科学研究科生物機能科学専攻食品バイオ工学講座
Laboratory of Food Analysis, Institute of Food Biotechnology, Department of Bioscience and Biotechnology, Division of Bioresource and Bioenvironmental Sciences, Graduate School Kyushu University
九州大学大学院生物資源環境科学研究科生物機能科学専攻食品バイオ工学講座
Laboratory of Food Analysis, Institute of Food Biotechnology, Department of Bioscience and Biotechnology, Division of Bioresource and Bioenvironmental Sciences, Graduate School Kyushu University
九州大学大学院生物資源環境科学研究科生物機能科学専攻食品バイオ工学講座
Laboratory of Food Analysis, Institute of Food Biotechnology, Department of Bioscience and Biotechnology, Division of Bioresource and Bioenvironmental Sciences, Graduate School Kyushu University
九州大学大学院生物資源環境科学研究科生物機能科学専攻食品バイオ工学講座
Laboratory of Food Analysis, Institute of Food Biotechnology, Department of Bioscience and Biotechnology, Division of Bioresource and Bioenvironmental Sciences, Graduate School Kyushu University
Chicken extract was hydrolyzed with proteases for food industry. The hydrolyzed chicken extracts and other chicken bouillons were tested for inhibitory activity against angiotensin Ⅰ converting enzyme (ACE). The hydrolyzate (ALC-1) treated with alcalase for 15h at 40℃ has the highest inhibitory activity against ACE. The IC_50-value of ACL-1 was 0.05mg-powder/ml. The ACL-1 was applied on a column packed with ODS resin and washed with water in order to remove salts and the water-soluble fraction. The most active fraction (E2) was eluted with 10% ethanol and showed the IC_50-value of 0.0024mg-powder/ml. A peptide that inhibited ACE was isolated from E2 by use of different modes of chromatography involving SP-Sephadex C-25 and reversed-phase HPLC. The amino acid sequence and the IC_50-value of the isolated peptide were Gly-Ala-Pro-Gly and 408μM, respectively.