ArticleInternational journal of molecular sciences2015
Characterization of peptides found in unprocessed and extruded amaranth (Amaranthus hypochondriacus) pepsin/pancreatin hydrolysates.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- Protein Fraction and Derived Peptides fromInternational journal of molecular sciences · 2026Article
- Exploring bioactive peptides from Andean grains and their potential applications: a review.Frontiers in nutrition · 2026Review
- A selection of African traditional and emerging foods: processing, composition, nutritional, sensory and nutraceutical aspects.Current research in food science · 2025Review
- Purification, Structural Characterization, and Bioactivity ofMolecules (Basel, Switzerland) · 2024Article
- Extrusion Improves the Antihypertensive Potential of a Kabuli Chickpea (Foods (Basel, Switzerland) · 2022Article
- Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates.Food chemistry: X · 2021Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The objectives of this study were to characterize peptides found in unprocessed amaranth hydrolysates (UAH) and extruded amaranth hydrolysates (EAH) and to determine the effect of the hydrolysis time on the profile of peptides produced. Amaranth grain was extruded in a single screw extruder at 125 °C of extrusion temperature and 130 rpm of screw speed. Unprocessed and extruded amaranth flour were hydrolyzed with pepsin/pancreatin enzymes following a kinetic at 10, 25, 60, 90, 120 and 180 min for each enzyme. After 180 min of pepsin hydrolysis, aliquots were taken at each time during pancreatin hydrolysis to characterize the hydrolysates by MALDI-TOF/MS-MS. Molecular masses (MM) (527, 567, 802, 984, 1295, 1545, 2034 and 2064 Da) of peptides appeared consistently during hydrolysis, showing high intensity at 10 min (2064 Da), 120 min (802 Da) and 180 min (567 Da) in UAH. EAH showed high intensity at 10 min (2034 Da) and 120 min (984, 1295 and 1545 Da). Extrusion produced more peptides with MM lower than 1000 Da immediately after 10 min of hydrolysis. Hydrolysis time impacted on the peptide profile, as longer the time lower the MM in both amaranth hydrolysates. Sequences obtained were analyzed for their biological activity at BIOPEP, showing important inhibitory activities related to chronic diseases. These peptides could be used as a food ingredient/supplement in a healthy diet to prevent the risk to develop chronic diseases.
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