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

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

Author information

1
Guangxi University of Science and Technology, Liuzhou, 545006, Guangxi, China. wusg1974@163.com.
2
Guangxi University of Science and Technology, Liuzhou, 545006, Guangxi, China.
3
Guangxi University of Science and Technology, Liuzhou, 545006, Guangxi, China. tianyuhonggx@163.com.

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

PMID:
28791512
DOI:
10.1007/s00726-017-2475-5
[Indexed for MEDLINE]

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