Journal
EUROPEAN FOOD RESEARCH AND TECHNOLOGY
Volume 240, Issue 1, Pages 137-145Publisher
SPRINGER
DOI: 10.1007/s00217-014-2315-8
Keywords
Abalone Haliotis Discus Hannai Ino; Gonads; ACE inhibitory peptide; Purification; Gastrointestinal digestion
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Funding
- National Natural Scientific Foundation of China [31271838]
- Ministry of Science and Technology of China [2012BAD38B09]
- Public Science and Technology Research Fund Project of Ocean [201305015-3]
- Science and Technology Bureau of Xiamen [3502Z20133020]
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Abalone gonads were hydrolyzed using alcalase followed by papain to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. Gel filtration column chromatography analysis showed that the molecular weight of the fraction with high ACE inhibitory activity was below 1 kDa, which occupied 93.1 % of total hydrolysate. The ACE inhibitory peptide was purified by a series of column chromatographies, and the sequence of purified peptide was further identified as Ala-Met-Asn (AMN) by automated Edman degradation method. The triple peptide was then synthesized and had an ACE inhibitory activity with IC50 value of 106.24 mu g/mL. After gastrointestinal digestion, the peptide still remained bioactivity. Lineweaver-Burk plots indicated that AMN acts as a non-competitive inhibitor against ACE. Our present study suggested that AMN derived from abalone gonad by-products may be used as an ideal nutrient for development of functional foods.
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