Structure elucidation of ACE-inhibitory and antithrombotic peptides isolated from mackerel skin gelatine hydrolysates

Authors

  • Zied Khiari,

    Corresponding author
    1. School of Food Science and Environmental Health, Dublin Institute of Technology (DIT), Dublin 1, Ireland
    • Correspondence To: Zied Khiari, School of Food Science and Environmental Health, Dublin Institute of Technology (DIT), Cathal Brugha Street, Dublin 1 Ireland. E-mail: khiari@ualberta.ca

    Search for more papers by this author
    • Current address: Department of Agricultural Food & Nutritional Science (AFNS), 4-10 Agriculture/Forestry Centre, University of Alberta, Edmonton, AB T6G 2P5, Canada

  • Daniel Rico,

    1. Agricultural Technological Institute of Castilla and Leon, Government of Castilla and Leon, Finca Zamaduenas, Valladolid, Spain
    Search for more papers by this author
  • Ana Belen Martin-Diana,

    1. Agricultural Technological Institute of Castilla and Leon, Government of Castilla and Leon, Finca Zamaduenas, Valladolid, Spain
    Search for more papers by this author
  • Catherine Barry-Ryan

    1. School of Food Science and Environmental Health, Dublin Institute of Technology (DIT), Dublin 1, Ireland
    Search for more papers by this author

Abstract

BACKGROUND

The fish-processing industry generates significant amounts of waste and by-products that are usually discarded. This study investigated the preparation of bioactive gelatine peptides from fish skin. Gelatine was extracted from mackerel (Scomber scombrus) skin and hydrolysed by pepsin for 1, 2, 6 and 24 h. All hydrolysates were screened for antioxidant, ACE-inhibitory and antithrombotic activities.

RESULTS

Gelatine peptides obtained after 24 h of hydrolysis exhibited the highest antioxidant activity (DPPH reduction ∼80%, FRAP ∼130 µmol Trolox equivalent L−1). These hydrolysates had high ACE-inhibitory activity (>70%) and were able to significantly (P < 0.05) inhibit platelet aggregation by about 30%, corresponding to moderate antithrombotic activity.

CONCLUSION

The bioactive properties were mainly due to the presence of low-molecular-weight peptides of 337 and 423 Da. © 2013 Society of Chemical Industry

Ancillary