Purification of angiotensin I-converting enzyme (ACE) inhibitory peptides from casein hydrolysate by IMAC-Ni2

Amino Acids. 2017 Oct;49(10):1787-1791. doi: 10.1007/s00726-017-2475-5. Epub 2017 Aug 8.

Abstract

Casein proteins were hydrolyzed by papain to identify inhibitory peptides of angiotensin I-converting enzyme (ACE). The hydrolysate was fractionized by immobilized metal affinity chromatography (IMAC-Ni2+). The fraction with high ACE inhibitory activity was enriched and further chromatographed on a reverse-phase column to yield four fractions. Among the fractions, the L4 fraction exhibited the highest ACE inhibitory activity and was identified by sequence analysis as Trp-Tyr-Leu-His-Tyr-Ala (WYLHYA), with IC50 value of 16.22 ± 0.83 µM in vitro. This peptide was expected to be applied as an ingredient for preventing hypertension and IMAC-Ni2+ may provide a simple method for purification of ACE inhibitory peptides.

Keywords: ACE inhibitory peptide; Casein hydrolysate; IMAC-Ni2+; Purification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors* / chemistry
  • Angiotensin-Converting Enzyme Inhibitors* / isolation & purification
  • Caseins / chemistry*
  • Chromatography, Affinity / methods
  • Humans
  • Peptides* / chemistry
  • Peptides* / isolation & purification
  • Peptidyl-Dipeptidase A / chemistry*

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Caseins
  • Peptides
  • casein hydrolysate
  • ACE protein, human
  • Peptidyl-Dipeptidase A