| Literature DB >> 25466072 |
Abraham T Girgih1, Rong He2, Fida M Hasan3, Chibuike C Udenigwe4, Tom A Gill3, Rotimi E Aluko5.
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.Entities:
Keywords: Antioxidant peptides; Cod; HPLC; Membrane ultrafiltration; Protein digestion
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Year: 2014 PMID： 25466072 DOI： 10.1016/j.foodchem.2014.10.079
Source DB: PubMed Journal: Food Chem ISSN： 0308-8146 Impact factor: 7.514