Purification and Synthesis of ACE Inhibitory Peptide from Acaudina molpadioidea Protein Hydrolysate

doi:10.3969/j.issn.0251-0790.2012.02.017

Abstract

Abstract: A novel ACE inhibitory peptide was isolated from the sea cucumber(Acaudina molpadioidea) hydrolysate using the chromatographic methods including gel filtration, ion-exchange chromatography and reversed phase high-performance liquid chromatography. The purified ACE inhibitory peptide was sequenced as MEGAQEAQGD, with a IC₅₀ value of 15.9 μmol/L. The ACE inhibitory peptide was synthesized by a method of gradual condensation and fragmental condensation. The purity of the decapeptide was 99.72%, and the molecular weight and sequence structure of the decapeptide equate with the fact. It was found that the inhibitory activity of the peptide was intensified by 3.5 times after incubation with pepsin and chymotrypsin. The ACE inhibitory peptide from Acaudina molpadioidea showed a clear antihypertensive effect on spontaneously hypertensive rats(SHR), at a dosage of 3 μmol/kg.

Key words: Acaudina molpadioidea, ACE inhibitory peptide, Isolation and purification

CLC Number:

O629.72

TrendMD:

ZHAO Yuan-Hui, LI Ba-Fang, MA Jing-Jun, DONG Shi-Yuan, LIU Zun-Ying, ZENG Ming-Yong. Purification and Synthesis of ACE Inhibitory Peptide from Acaudina molpadioidea Protein Hydrolysate[J]. Chem. J. Chinese Universities, 2012, 33(02): 308.

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