期刊
JOURNAL OF FUNCTIONAL FOODS
卷 5, 期 1, 页码 475-483出版社
ELSEVIER
DOI: 10.1016/j.jff.2012.12.003
关键词
Phascolosoma esculenta; Angiotensin I-converting enzyme inhibitor; Peptide; Purification; Spontaneously hypertensive rats
资金
- Fundamental Research Funds for the Central Universities, PR China
- National Major Science and Technology Projects of China, PR China [2012ZX09304009]
- Open Project Funding of Zhejiang Key Laboratory of Coastal Bio-resource, PR China [J2011001]
- Zhejiang Marine Biotechnology Innovation Team, PR China [2012R10029]
The water-soluble protein from Phascolosoma esculenta was hydrolyzed by pepsin to obtain the hydrolysate with angiotensin I-converting enzyme (ACE) inhibitory activity. The hydrolysate (PEPH) was then further separated by membrane bioreactor system, ion-exchange chromatography, gel filtration, and reversed phase high-performance liquid chromatography (RP-HPLC) and a novel ACE inhibitory peptide named as PeP with the IC50 value of 135 M was isolated. The amino acid sequence, Ala-Trp-Leu-His-Pro-Gly-Ala-Pro-Lys-Val-Phe, was identified by matrix-assisted laser desorption ionization-time of flight/time of flight (MALDI-TOF/TOF). Inhibitory kinetics study suggested that PeP acted as competitive inhibitor against ACE. Single oral administration of synthesized PeP at 10 mg/kg dose in spontaneously hypertensive rats could reduce the systolic blood pressure around 30 mmHg and the effect could last for more than 8 h. The results suggest that peptide from P. esculenta could be a potent natural ingredient for functional foods or pharmaceuticals against hypertension. (c) 2012 Elsevier Ltd. All rights reserved.
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