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KMID : 1007519970060020122
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Food Science and Biotechnology
1997 Volume.6 No. 2 p.122 ~ p.124
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Characterization of Angiotensin Converting Enzyme Inhibitor from Squid Hydrolysate
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Yang, Han Chul
Suh, Hyung Joo/Lee, Ho/Cho, Sung Ja/Whang, Jong Hyun
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Abstract
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Hydrolysates were prepared from squid with various proteases. Hydrolysates treated with pronase, actinase and actinidin showed a high inhibitory effect of ACE(Angiotensin Converting Enzyme). DH(Degree of Hydrolysis) increased with increasing hydrolysis time. The highest ACE inhibition effect was observed at 4 hour hydrolysis. Inhibitory peptide was purified from actinidin hydrolysate of squid by column chromatographies and HPLC. The purified inhibitor showed 0.6 ㎎/㎖ of IC_(50) value. The inhibitor showed the competitive inhibition patterns on ACE. The apparent Ki value of inhibitor for ACE was 2.39 mM with Hip-His-Leu as the substrate. The inhibitor of ACE was composed of Ala, Pro, Lys, Arg, Glu, Gly, Ile and Phe.
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