Potential ACE-inhibitory activity and nanoLC-MS/MS sequencing of peptides derived from aflatoxin contaminated peanut meal |
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Authors: | Brittany L White Timothy H Sanders Jack P Davis |
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Affiliation: | 1. Market Quality and Handling Research Unit, USDA ARS, North Carolina State University, 236 Schaub Hall, Raleigh, NC 27695, United States;2. Department of Food, Bioprocessing and Nutrition Sciences, North Carolina State University, Schaub Hall, Raleigh, NC 27695, United States |
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Abstract: | Our lab has developed a process for sequestering aflatoxin from contaminated peanut meal (PM) using commercial bentonite clays while protein is simultaneously extracted and hydrolyzed by a commercial protease. The objectives of this study were to sequence generated peptides and evaluate their potential ACE-inhibitory properties. Aflatoxin in the unprocessed PM was 610 μg kg−1 compared to 9.7 μg kg−1 on a dry weight basis in the 120 min hydrolysate. This hydrolysate displayed significant ACE-inhibitory activity with an IC50 of 295.1 μg mL−1. Ultrafiltration and size exclusion chromatography (SEC) improved the ACE-inhibitory properties, with the SEC fraction containing the smallest peptides having an IC50 = 44.4 μg mL−1. Additionally, 271 unique peptides were identified by nanoLC-MS/MS, of which 147 belonged to major seed storage proteins. This advanced characterization data will ultimately allow for more efficient production of hydrolysates with ACE-inhibitory activity or other bioactivities of interest from PM. |
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Keywords: | ACE-inhibitory Aflatoxin Bioactive peptides Peanut meal |
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