Antioxidant and ACE Inhibitory Activity of Enzymatic Hydrolysates from Ruditapes philippinarum

Molecules. 2018 May 16;23(5):1189. doi: 10.3390/molecules23051189.

Abstract

Ruditapes philippinarum proteins were hydrolyzed by trypsin, neutrase, and pepsin. The antioxidant activities and ACE inhibitory activity of hydrolysates were analyzed and the antioxidant activities were related to their molecular weight distribution and amino acid compositions. Results indicated the hydrolysis of proteins led to an increase in small peptides and free amino acids. The antioxidant activities of Ruditapes philippinarum hydrolysates against DPPH radical scavenging, inhibition on linoleic acid peroxidation, and reducing power showed that the neutrase hydrolysate exhibited the strongest antioxidant activity. In addition, an ACE inhibition assay revealed that the pepsin hydrolysate had the highest ACE inhibitory ability. Ruditapes philippinarum protein hydrolysates could be a promising source of natural antioxidant and ACE inhibitory.

Keywords: ACE inhibitory; Ruditapes philippinarum; amino acid composition; antioxidant activity; hydrolysates; molecular weight distribution.

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / pharmacology*
  • Animals
  • Antioxidants / pharmacology*
  • Bivalvia / metabolism*
  • Hydrolysis
  • Linoleic Acid / pharmacology
  • Lipid Peroxidation / drug effects
  • Molecular Weight
  • Pepsin A / metabolism
  • Peptides / pharmacology*
  • Proteins / chemistry*

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Antioxidants
  • Peptides
  • Proteins
  • Linoleic Acid
  • Pepsin A