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KMID : 1007520000090030163
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Food Science and Biotechnology
2000 Volume.9 No. 3 p.163 ~ p.167
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Purification and Identification of Angiotensin - 1 Converting Enzyme Inhibitory Compounds from Watercress (Nasturtium officinale)
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SHIN, HYUN KYUNG
KWON, IK BOO/Yang, Cha Bum/Park, Eun Jin/Lee, Hyeong Gyu/Park, Hyung Hwan
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Abstract
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Angiotensin-I converting enzyme (ACE) inhibitor was isolated from a Korean spice herb watercress (Nasturtium officinale), and its structure was identified. The 60% acetone-soluble extract from watercress showed 52.32% ACE inhibitory activity. The activity of n-butanol extract separated from 60% acetone extract increased (62.48%), while that of water or ethylacetate extract decreased. For isolation of ACE inhibitory compound, column chromatographies such as amberlite XAD-2, silicagel G60, sephadex LH-20, and high performance liquid chromatography (HPLC) were performed. The obtained active fraction had four main peaks. The highest active compound (P-4) had no reaction with ninhydrin reagent, indicating that the compound was not an amino acid or peptide, while the remaining three peaks were reactive with the same reagent. The molecular mass of P-4 using FAB-mass spectrometer and its chemical structure through the spectral data of UV absorption scanning and NMR spectrometries were identified as 267 and adenosine, respectively. This was the first result in which adenosine compound from plants extraction was found to have an ACE inhibitory effect.
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KEYWORD
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