Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Purification and Characterization of Angiotensin I Converting Enzyme lnhibitory Peptides from Enzymatic Hydrolysate of Cod Liver Protein

대구의 간 단백질의 효소적 가수분해물로부터 안지오텐신 I 전환효소 저해 펩타이드의 분리.정제 및 특성

  • Published : 2000.04.01
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Abstract

In order to utilize marine processing waste which would normally be discarded, cod liver protein was hydrolysed by ${\alpha}$-chymotrysin, and the hydrolysate was investigated for the new angiotensin I converting enzyme (ACE) inhibitor. Thy hydrolysate was separated into three major types, with molecular weight cut-off (MWCO) values less than 10 kDa, 5 kDa and 1 kDa of ultrafiltration membranes, respectively. ACE inhibitory peptides were isolated from the fractions passed through MWCO 1 kDa membrane, and purified by using ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, and HPLC on an ODS column. The purity was identified with capillary electrophoresis. The amino acid sequences of two peptides were Met-Ile-Pro-Pro-Tyr-Tyr (IC50=10.9 ${\mu}$M) and Gly-Leu-Arg-Asn-Gly-Ile (IC50=35.0 ${\mu}$M)

Keywords

References

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