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KMID : 1134820090380020177
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Journal of the Korean Society of Food Science and Nutrition
2009 Volume.38 No. 2 p.177 ~ p.181
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Characteristics of Angiotensin Converting Enzyme Inhibitory Peptides from Aroase AP10 Hydrolysate of Octopus
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Park Yeung-Beom
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Abstract
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The peptides from Aroase AP10 enzymatic hydrolysates of octopus proteins were isolated and tested for inhibitory activity against angiotensin converting enzyme (ACE). The Aroase AP10 hydrolysates were filtered through PM-10 membrane (M.W. cut-off 10,000) to obtain the peptides fractions with ACE inhibition activity. These fractions were applied to a Biogel P-2 column. Three active fractions (A, B, and C) were collected and applied to a SuperQ-Toyopearl 650S column chromatography, leading to the isolation of four active fractions (A-1, A-2, B-1, and C-1). Among the active fractions, C-1 had the highest ACE inhibitory activity (). The main composition of its amino acids is arginine, lysine, histidine and leucine, which cover about 60% of the total amino acids.
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KEYWORD
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angiotensin converting enzyme, octopus, Aroase AP10 hydrolysate
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