Neves, AC,Harnedy, PA,O'Keeffe, MB,FitzGerald, RJ

2017

March

Food chemistry

Bioactive peptides from Atlantic salmon (Salmo salar) with angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory, and antioxidant activities

Published

()

Salmon trimmings Bioactive peptides ACE DPP-IV ORAC Simulated gastrointestinal digestion Protein extraction Protein hydrolysates BETA-LACTOGLOBULIN WHEY-PROTEIN BY-PRODUCTS MUSCLE IDENTIFICATION HYDROLYSATE ACID STABILITY SHELLFISH PROTEASES

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The pH shift method was utilised for the recovery of proteins from salmon trimmings (ST), yielding 93% (w/w) protein. ST protein (STP) hydrolysates were generated with different enzyme preparations. STP incubated with Corolase PP for 1 h (STP-C1) had the most potent angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory and oxygen radical absorbance capacity (ORAC) activities. Analysis of fractions of STP-C1 using UPLC-MS/MS identified sixteen peptides/amino acids. Tyr-Pro had the highest ACE inhibitory activity (ACE IC50 = 5.21 +/- 0.94 mu M). The highest DPP-IV inhibitory activity was found with the amino acid Tyr (DPP-IV IC50 = 75.15 +/- 0.84 mu M). Val-Pro had the highest ORAC activity (19.45 +/- 2.15 mu mol of TE g(-1)). To our knowledge, the peptides Gly-Pro-Ala-Val, Val-Cys, and Phe-Phe have not been previously identified to have the activities tested in this study. These results indicate that STP hydrolysates are potential sources of bioactive peptides. (C) 2016 Elsevier Ltd. All rights reserved.

10.1016/j.foodchem.2016.09.053