Angiotensin-Converting Enzyme Inhibition In Vitro by Protein Hydrolysates and Peptide Fractions From Mojarra of Nile Tilapia (Oreochromis Niloticus) Skeleton

J Med Food. 2019 Mar;22(3):286-293. doi: 10.1089/jmf.2018.0163. Epub 2019 Mar 5.

Abstract

Mojarra of Nile tilapia (Oreochromis niloticus) skeleton was used as protein source for the preparation of protein hydrolysates and peptide fractions with angiotensin-converting enzyme (ACE) inhibitory activity. The flour presented a content of 34.92% protein and a brightness (luminosity, L*) of 82.29. Protein hydrolysates were obtained from the protein-rich flour with the enzymes Flavourzyme® and Alcalase® reaching degree of hydrolysis (%DH) of 52% and 67% at 100 min of reaction, respectively. Both hydrolysates showed low-molecular-weight (MW) peptides estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The hydrolysates obtained with Flavourzyme at 60 min and at 80 min with Alcalase showed greater ACE inhibitory activity with IC50 values of 0.238 and 0.344 mg/mL, respectively. The peptide fraction A (MW >10 kDa) with Flavourzyme and fraction B (MW = 10-5 kDa) with Alcalase obtained by ultrafiltration of hydrolysates with higher DH presented IC50 of 0.728 and 0.354 mg/mL, respectively, whereas peptide fraction C (MW = 5-3 kDa) with both enzymes hydrolysates with greater ACE inhibitory activity showed IC50 values of 0.470 and 0.634 mg/mL. The components obtained in this study could be used as functional ingredients in the design and development of functional foods.

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry*
  • Animals
  • Antihypertensive Agents / chemistry*
  • Biocatalysis
  • Cichlids*
  • Fish Proteins / chemistry*
  • Hydrolysis
  • Kinetics
  • Peptides / chemistry*
  • Peptidyl-Dipeptidase A / chemistry
  • Protein Hydrolysates / chemistry
  • Subtilisins / chemistry

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Antihypertensive Agents
  • Fish Proteins
  • Peptides
  • Protein Hydrolysates
  • Peptidyl-Dipeptidase A
  • Subtilisins