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Angiotensin I-converting enzyme inhibitory activity in a hydrolysate of proteins from Northern shrimp (Pandalus borealis) and identification of two novel inhibitory tri-peptides

Authors
Journal
Process Biochemistry
1359-5113
Publisher
Elsevier
Volume
46
Issue
11
Identifiers
DOI: 10.1016/j.procbio.2011.08.003
Keywords
  • Shrimp Protein Hydrolysate
  • Pandalus Borealis
  • Ace Inhibitory Activity
  • Nutraceutical
Disciplines
  • Biology

Abstract

Abstract The ACE inhibitory activity of a desalted protein hydrolysate from Northern shrimp (Pandalus borealis) was studied. Measurements by two independent methods both revealed higher in vitro ACE inhibitory activity, IC50=0.075 and 0.035mg/ml, respectively, than earlier reported in comparable hydrolysates. Two novel ACE inhibitory tri-peptides, Phe-Thr-Tyr (IC50=275 and 59μM) and Phe-Ser-Tyr (IC50=7.7 and 2.2μM), were detected in the hydrolysate. An introductory feeding trial with spontaneously hypertensive rats indicated positive in vivo results when the rats were given 60mg hydrolysate/kg body weight per day. Although further in vivo studies are necessary to verify the antihypertensive potential, the very high in vitro ACE inhibitory activity reveals that the shrimp protein hydrolysate is a promising candidate for nutraceutical application.

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