Characterization of Protein Hydrolysates from Fish Discards and By-Products from the North-West Spain Fishing Fleet as Potential Sources of Bioactive Peptides

Mar Drugs. 2021 Jun 13;19(6):338. doi: 10.3390/md19060338.

Abstract

Fish discards and by-products can be transformed into high value-added products such as fish protein hydrolysates (FPH) containing bioactive peptides. Protein hydrolysates were prepared from different parts (whole fish, skin and head) of several discarded species of the North-West Spain fishing fleet using Alcalase. All hydrolysates had moisture and ash contents lower than 10% and 15%, respectively. The fat content of FPH varied between 1.5% and 9.4% and had high protein content (69.8-76.6%). The amino acids profiles of FPH are quite similar and the most abundant amino acids were glutamic and aspartic acids. All FPH exhibited antioxidant activity and those obtained from Atlantic horse mackerel heads presented the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, reducing power and Cu2+ chelating activity. On the other hand, hydrolysates from gurnard heads showed the highest ABTS radical scavenging activity and Fe2+ chelating activity. In what concerns the α-amylase inhibitory activity, the IC50 values recorded for FPH ranged between 5.70 and 84.37 mg/mL for blue whiting heads and whole Atlantic horse mackerel, respectively. α-Glucosidase inhibitory activity of FPH was relatively low but all FPH had high Angiotensin Converting Enzyme (ACE) inhibitory activity. Considering the biological activities, these FPH are potential natural additives for functional foods or nutraceuticals.

Keywords: ACE inhibitory activity; Fe2+ chelating activity; bioactive peptides; radical scavenging activity; α-amylase and α-glucosidase inhibitory activities.

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors* / analysis
  • Angiotensin-Converting Enzyme Inhibitors* / chemistry
  • Angiotensin-Converting Enzyme Inhibitors* / isolation & purification
  • Angiotensin-Converting Enzyme Inhibitors* / pharmacology
  • Animals
  • Antihypertensive Agents* / analysis
  • Antihypertensive Agents* / chemistry
  • Antihypertensive Agents* / isolation & purification
  • Antihypertensive Agents* / pharmacology
  • Antioxidants* / analysis
  • Antioxidants* / chemistry
  • Antioxidants* / isolation & purification
  • Antioxidants* / pharmacology
  • Biological Products / analysis
  • Biological Products / chemistry
  • Biological Products / isolation & purification
  • Biological Products / pharmacology
  • Fish Proteins* / analysis
  • Fish Proteins* / chemistry
  • Fish Proteins* / isolation & purification
  • Fish Proteins* / pharmacology
  • Fisheries
  • Fishes
  • Glycoside Hydrolase Inhibitors* / analysis
  • Glycoside Hydrolase Inhibitors* / chemistry
  • Glycoside Hydrolase Inhibitors* / isolation & purification
  • Glycoside Hydrolase Inhibitors* / pharmacology
  • Iron Chelating Agents* / analysis
  • Iron Chelating Agents* / chemistry
  • Iron Chelating Agents* / isolation & purification
  • Iron Chelating Agents* / pharmacology
  • Molecular Weight
  • Protein Hydrolysates* / analysis
  • Protein Hydrolysates* / chemistry
  • Protein Hydrolysates* / isolation & purification
  • Protein Hydrolysates* / pharmacology
  • Spain

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Antihypertensive Agents
  • Antioxidants
  • Biological Products
  • Fish Proteins
  • Glycoside Hydrolase Inhibitors
  • Iron Chelating Agents
  • Protein Hydrolysates