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Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Wakame (Undaria pinnatifida) and Their Antihypertensive Effect in Spontaneously Hypertensive Rats
Abstract
Seven kinds of angiotensin I-converting enzyme (ACE) inhibitory peptides were isolated from the hydrolysates of wakame (Undaria pinnatifida) by Protease S "Amano" (from Bacillus stearothermophilus) by using three-step high-performance liquid chromatography (HPLC) on a reverse-phase column. These peptides were identified by amino acid composition analysis, sequence analysis, and liquid chromatography-mass spectrometry (LC-MS), as Val-Tyr (IC(50) = 35.2 microM), Ile-Tyr (6.1 microM), Ala-Trp (18.8 microM), Phe-Tyr (42.3 microM), Val-Trp (3.3 microM), Ile-Trp (1.5 microM), and Leu-Trp (23.6 microM). These peptides have resistance against gastrointestinal proteases in vitro. Each peptide was determined to have an antihypertensive effect after a single oral administration in spontaneously hypertensive rats (SHR). Among them, the blood pressure significantly decreased by Val-Tyr, Ile-Tyr, Phe-Tyr, and Ile-Trp in a dose of 1 mg/kg of body weight (BW). The present study showed that antihypertensive effect in the hydrolysates of wakame by Protease S "Amano" was attributed to these peptides.
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Metadata
- Authors
- Sato, M., Hosokawa, T., Yamaguchi, T., Nakano, T., Muramoto, K., Kahara, T., Funayama, K., Kobayashi, A., & Nakano, T.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-09-14
- Volume
- 50
- Issue
- 21
- Pages
- 6245-6252
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2087447071
- Cited by
- 290
- References
- 0
- FWCI
- 1.30
- Type
- journal article
- Language
- en
- Open access
- closed
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