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

• Main Authors: Lixia Sun, Shanguang Wu, Liqin Zhou, Feng Wang, Xiongdiao Lan, Jianhua Sun, Zhangfa Tong, Dankui Liao
• Format: Article
• Language: English
• Published: MDPI AG 2017-02-01
• Series: Marine Drugs
• Subjects: ACE-inhibitory activity; lizard fish; hydrolysate; purification; IMAC
• Online Access: http://www.mdpi.com/1660-3397/15/2/29

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.