Purification and structural identification of glutelin peptides derived from oats

Glutelins 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-s...

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Bibliographic Details
Published inCYTA: journal of food Vol. 15; no. 4; pp. 508 - 515
Main Authors Ma, Sarina, Zhang, Meili, Beta, Trust, Dong, Tungalag, Bao, Xiaolan, Li, Ziqin
Format Journal Article
LanguageEnglish
Published Abingdon Taylor & Francis 02.10.2017
Taylor & Francis Ltd
Taylor & Francis Group
Subjects
amino acid sequence
antioxidant peptides
Antioxidants
ESI-MS/MS
Glutelin
Hidrolizados de glutelina de avena
Hydrolysates
Ionization
Ions
Mass spectrometry
Mass spectroscopy
Oat glutelin hydrolysates
Oats
Peptides
Protein purification
Purification
péptidos antioxidantes
Scavenging
secuencia de aminoácidos
Subtilisin
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Summary:Glutelins 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).
ISSN:1947-6337
1947-6345
DOI:10.1080/19476337.2017.1301555