期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 61, 期 17, 页码 4097-4100出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf4001378
关键词
walnut; peptide; ACE-inhibitory activity; purification; characterization
资金
- Fundamental Research Funds for the Central Universities [HIT.BRE-TIII.201231]
- National Natural Science Foundation [31101316]
- Program of New Century Excellent Talents in University [NCET-11-0796]
- Innovative Talent of Science and Technology Fund in Harbin [2011RFQXN041]
In the present study, a novel angiotensin I-converting enzyme (ACE)-inhibitory peptide, P-2a2, was purified to homogeneity from walnut protein hydrolysate by ultrafiltration, consecutive column chromatography, and high-performance liquid chromatography. The purified peptide was characterized by matrix assisted laser desorption ionization time mass spectrophotometry and a liquid phase peptide sequencer. The molecular mass of P-2a2 was tested to be 1033.42 D. Its amino acid sequence was determined to be Trp-Pro-Glu-Arg-Pro-Pro-Gln-Ile-Pro. The potent ACE-inhibitory peptide is an enneapeptide and shows a high ACE inhibitory activity, with an IC50 value of 25.67 mu g/mL.
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