Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni2

Mar Drugs. 2017 Feb 15;15(2):29. doi: 10.3390/md15020029.

Abstract

Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish (Saurida elongata) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated from LFPH-I using immobilized metal affinity chromatography (IMAC-Ni2+). Analysis of amino acid levels revealed that F2 eluted from IMAC was enriched in Met, His, Tyr, Pro, Ile, and Leu compared to the crude peptide LFPH-I. F2 with the high ACE inhibitory activity (IC50 of 0.116 mg·mL-1) was further separated by a reverse-phase column to yield a novel ACE inhibitory peptide with IC50 value of 52 μM. The ACE inhibitory peptide was identified as Arg-Tyr-Arg-Pro, RYRP. The present study demonstrated that IMAC may be a useful tool for the separation of ACE inhibitory peptides from protein hydrolysate.

Keywords: ACE-inhibitory activity; IMAC; hydrolysate; lizard fish; purification.

Publication types

  • Evaluation Study

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry
  • Angiotensin-Converting Enzyme Inhibitors / isolation & purification*
  • Animals
  • Chemical Fractionation
  • Chromatography, Affinity / methods*
  • Chromatography, Reverse-Phase
  • Fish Proteins / chemistry
  • Fish Proteins / isolation & purification*
  • Fishes*
  • Oligopeptides / isolation & purification*
  • Protein Hydrolysates / chemistry*
  • Ultrafiltration

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Fish Proteins
  • Oligopeptides
  • Protein Hydrolysates