Abstract
ABSTRACTGlutelins derived from oats were purified and hydrolyzed sequentially using alcalase proteases for production of antioxidant peptides. The antioxidant activities of oat glutelin peptides were evaluated using reducing power methods including hydroxyl and 1,1-diphenyl-2-pycrylhydrazyl (DPPH) radical-scavenging assays. The results demonstrated that oats glutelin peptide D-1a exhibited the highest antioxidant activity compared to the other hydrolysates. D-1a was identified to be His–Tyr–Asn–Ala–Pro–Ala–Leu (784.38 Da) by electrospray ionization mass spectrometry (ESI-MS/MS).
Highlights
Proteins in oats have been shown to have high nutritional value and functional properties (Klose & Arendt, 2012)
Phengnuam et al (2013) studied the J. curcas seedcake protein hydrolysate and the IC50 of scavenging effect against DPPH radical was 3.31 mg mL−1. They came to conclusion that cottonseed protein peptide and protein hydrolysate of J. curcas seedcake had strong antioxidant activity
The antioxidative oat glutelin hydrolysate was further isolated in order to identify the antioxidant peptides
Summary
Proteins in oats have been shown to have high nutritional value and functional properties (Klose & Arendt, 2012). Oat glutelin hydrolysates have been shown to possess high antioxidant activity using in vitro analysis (Ma, Zhang, Bao, & Dong, 2014). The composition of oat protein molecules is complex and diverse, with variable sizes and structure. Protease treatment of these proteins can cause the formation of enzymatic hydrolysates which have potential bioactive functionalities. In order to characterize the functionalities of these enzymatic hydrolysates, they need to be isolated and purified to obtain specific active peptide fractions. For determining the relationship between the structure and bioactive functionalities, the active components of the isolated peptide fractions are required to be identified and characterized
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