4.7 Article

Isolation of an Antihypertensive Peptide from Alcalase Digest of Spirulina platensis

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 58, Issue 12, Pages 7166-7171

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf100193f

Keywords

Spirulina platensis; angiotensin I-converting enzyme; ACE inhibitory peptide; antihypertension

Funding

  1. China Scholarship Council [[2007]3021]
  2. Excellent Youth Scholars Special Innovation Program [BLY X200935]
  3. Beijing Forestry University [TD20 10-3]
  4. Japanese MEXT (Ministry of Education, Culture, Sports, Science and Technology)

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available