Isolation, purification and characterization of antioxidative peptide of pearl millet (Pennisetum glaucum) protein hydrolysate

•Perl millet protein hydrolysis with trypsin from porcine pancreas.•Peptide with a specific molecular weight showed a good antioxidant activity.•Peptide showed good metal chelating and hydroxyl radical scavenging activity.•Peptide exhibited good reducing power at 0.375nm.•Sequence SDRDLLGPNNQYLPK id...

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Bibliographic Details
Published in:Food chemistry 2016-08, Vol.204, p.365-372
Main Authors: Agrawal, Himani, Joshi, Robin, Gupta, Mahesh
Format: Article
Language:English
Subjects:
Antioxidant
Antioxidants - chemistry
Antioxidants - isolation & purification
Benzothiazoles - metabolism
Calorimetry, Differential Scanning
MALDI-TOF-MS
Molecular Weight
Pearl millet
Pennisetum - chemistry
Peptide purification
Peptides - chemistry
Peptides - isolation & purification
Protein Hydrolysates - chemistry
RP-UFLC
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Sulfonic Acids - metabolism
Tandem Mass Spectrometry
Trypsin - metabolism
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Summary:•Perl millet protein hydrolysis with trypsin from porcine pancreas.•Peptide with a specific molecular weight showed a good antioxidant activity.•Peptide showed good metal chelating and hydroxyl radical scavenging activity.•Peptide exhibited good reducing power at 0.375nm.•Sequence SDRDLLGPNNQYLPK identified by using MALDI-TOF-MS. Pearl millet (Pennisetum glaucum) is a rich source of protein, used for present study to hydrolyze protein, peptide separation and its functional activity. Antioxidative bioactive peptide was successfully identified from pearl millet using trypsin enzyme. Different antioxidative potential of isolated peptide were assessed based on activity of DPPH radical, ABTS radical, hydroxyl radical, Fe2+ chelating ability and reducing power. Bioactive peptide separated by gel-filtration chromatography, showed the higher antioxidant activity as tested by different free radicals. The activity of pearl millet protein hydrolysate fraction was found for DPPH assay (67.66%), ABTS assay (78.81%), Fe2+ chelating ability (51.20%), hydroxyl assay (60.95%) and reducing power (0.375nm) was further purified using reversed-phase UFLC and subjected to matrix assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/TOF-MS) for sequential identification of the peptide. The sequence SDRDLLGPNNQYLPK was identified as antioxidant peptide.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2016.02.127