Amino Acids

, Volume 49, Issue 10, pp 1787–1791 | Cite as

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

Short Communication

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

Casein hydrolysate IMAC-Ni2+ ACE inhibitory peptide Purification 

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Copyright information

© Springer-Verlag GmbH Austria 2017

Authors and Affiliations

  1. 1.Guangxi University of Science and TechnologyLiuzhouChina

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