Identification of antihypertensive peptides from peptic digest of two microalgae, Chlorella vulgaris and Spirulina platensis

被引：240

作者：

Suetsuna, K

Chen, JR

机构：

[1] Natl Fisheries Univ, Dept Food Sci & Technol, Shimonoseki, Yamaguchi 7596595, Japan

[2] Taipei Med Univ, Sch Nutr & Hlth Sci, Taipei 110, Taiwan

来源：

MARINE BIOTECHNOLOGY | 2001年 / 3卷 / 04期

关键词：

Chlorella vulgaris; Spirulina platensis; peptic digest; peptide; angiotensin I-converting enzyme; spontaneously hypertensive rat;

D O I：

10.1007/s10126-001-0012-7

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 [微生物学]; 0836 [生物工程]; 090102 [作物遗传育种]; 100705 [微生物与生化药学];

摘要：

The peptidic fractions that inhibited angiotensin 1-converting enzyme (ACE) were separated from the peptic digests of 2 microalgae, Chlorella vulgaris and Spirulina platensis, by ion exchange chromatography and gel filtration. Oral administration of peptidic fractions into spontaneously hypertensive rats at 200 mg/kg of body weight resulted in marked antihypertensive effects. Further separation of the peptidic fractions by ODS high-performance liquid chromatography furnished the following active peptides: Ile-Val-Val-Glu (inhibitory against ACE with an IC50 of 315.3 muM), Ala-Phe-Leu (63.8 muM), Phe-Ala-Leu (26.3 muM), Ala-Glu-Leu (57.1 muM), and Val-Val-Pro-Pro-Ala (79.5 muM) from C. vulgaris, Ile-Ala-Glu (34.7 muM), Phe-Ala-Leu, Ala-Glu-Leu, Ile-Ala-Pro-Gly (11.4 muM), and Val-Ala-Phe (35.8 muM) from S. platensis.

引用

页码：305 / 309

页数：5

共 21 条

[1]

ASTAWAN M, 1995, BIOSCI BIOTECH BIOCH, V59, P524

[2]

CHEUNG HS, 1980, J BIOL CHEM, V255, P401

[3]

INHIBITION O HOMOGENEOUS ANGIOTENSIN-CONVERTING ENZYME OF RABBIT LUNG BY SYNTHETIC VENOM PEPTIDES OF BOTHROPS-JARARACA [J].