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Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein
Peptides (2012)
  • Jiwang Chen
  • Yimei Wang
  • Qixin Zhong, University of Tennessee, Knoxville
  • Yongning Wu
  • Wenshui Xia
Abstract

Peptides inhibiting angiotensin-I converting enzyme (ACE, EC. 3.4.15.1) are possible cures of hypertension. Food-derived ACE-inhibitory peptides are particularly attractive because of reduced side effects. Previously, we reported ACE-inhibitory activity of grass carp protein hydrolysates. In this work, we report steps for purifying the ACE-inhibitory peptide from the hydrolysate and its biochemical properties. Following steps of ultrafiltration, macroporous adsorption resin, and two steps of reversed phase high performance liquid chromatography (RE-HPLC), a single Val-Ala-Pro (VAP) tripeptide was identified. The tripeptide with excellent ACE-inhibitory activity (IC50 value of 0.00534 mg/mL) was a competitive ACE inhibitor and stable against both ACE and gastrointestinal enzymes of pepsin and chymotrypsin. This is the first report of food-derived VAP. The identified unique biochemical properties of VAP may enable the application of grass carp protein hydrolysates as a functional food for treatments of hypertension. The developed purification conditions also allow the production of VAP for pharmaceutical applications. DOI: http://dx.doi.org/10.1016/j.peptides.2011.11.006

Keywords
  • Grass carp protein hydrolysate,
  • ACE-inhibitory peptide,
  • Purification,
  • Inhibition pattern,
  • Stability against gastrointestinal enzymes
Disciplines
Publication Date
January, 2012
Citation Information
Jiwang Chen, Yimei Wang, Qixin Zhong, Yongning Wu, et al.. "Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein" Peptides Vol. 33 Iss. 1 (2012)
Available at: http://works.bepress.com/qixin_zhong/5/