Evaluation of the in vitro antioxidant properties of a cod (Gadus morhua) protein hydrolysate and peptide fractions. (15th April 2015)

• Record Type: Journal Article
• Authors: Girgih, Abraham T.; He, Rong; Hasan, Fida M.; Udenigwe, Chibuike C.; Gill, Tom A.; Aluko, Rotimi E.
• Is Part Of: Food chemistry. Volume 173(2015)
• Page Start: 652
• Page End: 659
• Publication Date: 2015-04-15
• Subjects: Cod -- Protein digestion -- HPLC -- Antioxidant peptides -- Membrane ultrafiltration; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2014.10.079
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: A <1 kDa cod protein hydrolysate (CPH) was separated into 4 fractions by RP-HPLC. CPH had better hydroxyl and superoxide scavenging activities than RP-HPLC fractions. RP-HPLC fractions had better ORAC values and DPPH scavenging than the CPH. Inhibition of linoleic acid peroxidation by CPH and fractions was dose-dependent. Abstract: Mechanically-deboned cod muscle proteins were sequentially hydrolysed using pepsin and a trypsin + chymotrypsin combination, which was followed by passing the digest through a 1 kDa equipped tangential flow filtration system; the permeate (<1 kDa peptides) was collected as the cod protein hydrolysate (CPH). Reversed-phase high performance liquid chromatography (RP-HPLC) was used to separate the CPH into four peptide fractions (CF1–CF4) and their in vitro antioxidant properties investigated. Results showed that most of the peptide fractions (CF2–CF4) displayed significantly higher ( p < 0.05) oxygen radical absorbance capacity values (698–942 μM Trolox equivalents, TE/g) and 2, 2-diphenyl-1-picrylhydrazyl scavenging activities (17–32%) than those of CPH (613 μM TE/g and 19%, respectively). However, the unfractionated CPH displayed improved capability to scavenge superoxide and hydroxyl radicals as well as significantly higher ( p < 0.05) ferric iron reduction and chelation of iron than the RP-HPLC peptides. The CPH and peptide fractions displayed a dose-dependent inhibition of linoleic acid oxidation.