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

Kunio Suetsuna; Jiun-Rong Chen

doi:10.1007/s10126-001-0012-7

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

Kunio Suetsuna, Jiun-Rong Chen

Research output: Contribution to journal › Article

111 Citations (Scopus)

Abstract

The peptidic fractions that inhibited angiotensin I-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 μM), Ala-Phe-Leu (63.8 μM), Phe-Ala-Leu (26.3 μM), Ala-Glu-Leu (57.1 μM), and Val-Val-Pro-Pro-Ala (79.5 μM) from C. vulgaris; Ile-Ala-Glu (34.7 μM), Phe-Ala-Leu, Ala-Glu-Leu, Ile-Ala-Pro-Gly (11.4 μM), and Val-Ala-Phe (35.8 μM) from S. platensis.

Original language	English
Pages (from-to)	305-309
Number of pages	5
Journal	Marine Biotechnology
Volume	3
Issue number	4
DOIs	https://doi.org/10.1007/s10126-001-0012-7
Publication status	Published - 2001

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Keywords

Angiotensin I-converting enzyme
Chlorella vulgaris
Peptic digest
Peptide
Spirulina platensis
Spontaneously hypertensive rat

ASJC Scopus subject areas

Aquatic Science
Biotechnology

Cite this

Suetsuna, K., & Chen, J-R. (2001). Identification of antihypertensive peptides from peptic digest of two microalgae, Chlorella vulgaris and Spirulina platensis. Marine Biotechnology, 3(4), 305-309. https://doi.org/10.1007/s10126-001-0012-7

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abstract = "The peptidic fractions that inhibited angiotensin I-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 μM), Ala-Phe-Leu (63.8 μM), Phe-Ala-Leu (26.3 μM), Ala-Glu-Leu (57.1 μM), and Val-Val-Pro-Pro-Ala (79.5 μM) from C. vulgaris; Ile-Ala-Glu (34.7 μM), Phe-Ala-Leu, Ala-Glu-Leu, Ile-Ala-Pro-Gly (11.4 μM), and Val-Ala-Phe (35.8 μM) from S. platensis.",

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AB - The peptidic fractions that inhibited angiotensin I-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 μM), Ala-Phe-Leu (63.8 μM), Phe-Ala-Leu (26.3 μM), Ala-Glu-Leu (57.1 μM), and Val-Val-Pro-Pro-Ala (79.5 μM) from C. vulgaris; Ile-Ala-Glu (34.7 μM), Phe-Ala-Leu, Ala-Glu-Leu, Ile-Ala-Pro-Gly (11.4 μM), and Val-Ala-Phe (35.8 μM) from S. platensis.

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10.1007/s10126-001-0012-7