期刊
EUROPEAN FOOD RESEARCH AND TECHNOLOGY
卷 239, 期 2, 页码 333-338出版社
SPRINGER
DOI: 10.1007/s00217-014-2227-7
关键词
Walnut; Peptide; ACE-inhibitory activity; Purification; Identification
资金
- Fundamental Research Funds for the Central Universities [HIT.BRETIII.201231]
- National Natural Science Foundation [31101316, 31371805]
- Program of New Century Excellent Talents in University [NCET-11-0796]
- Innovative Talent of Science and Technology Fund in Harbin [2011RFQXN041]
Angiotensin I-converting enzyme (ACE) is a dipeptidyl carboxypeptidase. It plays an important physiological role in regulating blood pressure in human bodies. ACE-inhibitory peptides inhibit the activity of ACE, thereby decreasing the tension of blood vessels and the blood volume, thus lowering blood pressure. ACE-inhibitory peptides derived from food proteins due to their safety properties and beneficial effects on human health have attracted more and more attentions on their ACE-inhibitory activity. In the present study, a novel ACE-inhibitory peptide, P-1a1, was homogeneously purified from walnut protein hydrolysate by ultrafiltration, consecutive column chromatography and high performance liquid chromatography. The purified peptide was characterized by Edman degradation, matrix-assisted laser desorption ionization time-of-flight mass spectrophotometer and a liquid-phase peptide sequencer. The amino acid sequence of P-1a1 was determined to be LPGRPPIKPWPL. The potent ACE-inhibitory peptide showed a high ACE-inhibitory activity with the IC50 value of 128.98 mu g/mL (95.2 mu mol/L). The purified peptide could be used in functional food products as a bioactive component with good ACE-inhibitory activity.
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