The objective was to investigate the antioxidant potential of peptides derived from the enzymatic hydrolysis of a mung bean (Vigna radiata) albumin fraction using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) enhancer (ABTS) radical scavenging assay, a Fe2+ chelating assay, and an oxygen radical absorbance capacity (ORAC) assay. Peeled, raw mung beans were ground into flour, mixed with sodium borate buffer (pH 8.3) at 1:20 (w/v) ratio, stirred, and filtered using a 30 kDa molecular weight cut-off centrifugal filter to obtain an albumin fraction. A manual theoretical hydrolysis of the mung bean albumin sequences in the UniProt database was performed using alcalase, stem bromelain, ficin, papain, and thermolysin using the specificity data in the MEROPS database to determine potentially antioxidant peptides. The albumin fraction obtained underwent enzymatic hydrolysis using gastrointestinal enzymes (GI) and thermolysin. Protein and peptide profiles were evaluated using SDS-PAGE and LC-ESI-MS/MS. Bioactive fragments present in mung bean albumin sequences were identified using the BIOPEP database. Albumin peptides showed low ABTS radical-scavenging activity (6-7%), but high Fe2+-binding activity (80-90%) and high ORAC value (&gt;130 μM Trolox equivalents) in comparison to known antioxidants. Thermolysin produced small di-/tri- peptides sequences (lys-lys, asp-met) with high hydrophobicity and low molecular mass that showed higher antioxidant capacity compared to peptides obtained from GI hydrolysis. In conclusion, mung bean albumin peptides enzymatically produced by two different schemes had antioxidant capacity defined by their molecular mass, hydrophobicity, amino acid composition and sequence.

Antioxidant potential of mung bean (Vigna radiata) albumin peptides produced by enzymatic hydrolysis and analyzed by biochemical and in silico methods

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.