Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 58, Issue 12, Pages 7166-7171Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf100193f
Keywords
Spirulina platensis; angiotensin I-converting enzyme; ACE inhibitory peptide; antihypertension
Funding
- China Scholarship Council [[2007]3021]
- Excellent Youth Scholars Special Innovation Program [BLY X200935]
- Beijing Forestry University [TD20 10-3]
- Japanese MEXT (Ministry of Education, Culture, Sports, Science and Technology)
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An angiotensin I-converting enzyme (ACE) inhibitory peptide lie-Gin-Pro with an IC(50) value of 5.77 +/- 0.09 mu M was purified from the alcalase digests of Spirulina platensis by gel filtration chromatography and two steps of reverse-phase high-performance liquid chromatography (RP-HPLC). The peptide was synthesized and showed resistance to in vitro digestion by gastrointestinal proteases. Kinetics studies indicated that the peptide was a noncompetitive inhibitor and that the K(i) value was 7.61 +/- 0.16 mu M. Oral administration of lie-Gin-Pro at a dosage of 10 mg/kg showed significant decreases of the weighted systolic blood pressure (SBP) and diastolic blood pressure (DBP) in spontaneously hypertensive rats (SHR) at 4, 6, and 8 h after treatment. The results showed that the ACE inhibitory peptide from Spirulina platensis may have potential for use in the prevention and treatment of hypertension.
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