KMID : 1134820000290040719
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Journal of the Korean Society of Food Science and Nutrition 2000 Volume.29 No. 4 p.719 ~ p.725
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Purification and Characterization of Angiotensin I - Converting Enzyme Inhibitor from Porphyra yezoensis
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Choi Soo-Jin
Jun Woo-Jin Yoo Kwang-Won Shin Dong-hoon Hong Bum-Shik Cho Hong-Yon Yang Han-Chul
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Abstract
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This study focused on the purification and characterization of ACE inhibitor from Porphyra yezoensis. The dried Porphyra yezoensis was ground and hydrolyzed with 2.5 N HCl, followed by neutralization and centrifugation. Then, the subsequential purification of ACE inhibitor was carried out by Amberlite XAD 8, DEAE-Toyopearl 650C, Sephadex LH-20 column chromatography and reverse phase HPLC with C_(18) column. The purified ACE inhibitor was peptide which consisted of glycine (24.5%), arginine (56.8%) and proline (18.8%). Also, it showed the competitive inhibition pattern to ACE. The apparent molecular mass of purified peptide was 580 dalton, and an IC50 value of ACE inhibitor was 10.6 ¥ìg.
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KEYWORD
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angiotensin I-converting enzyme (ACE), peptide, Porphyra yezonensis
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