Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies
Cold press technology generates high quality value-added oil products along with highly stable oilseed cakes. Hazelnut cakes are characterized by high protein concentrations that can be industrially valorized. Here, using an aqueous extraction scheme along with enzymatic proteolysis and FPLC (fast p...
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| Autores principales: | , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Elsevier
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/29f649acecc64ed9ada69a13532f3924 |
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| Sumario: | Cold press technology generates high quality value-added oil products along with highly stable oilseed cakes. Hazelnut cakes are characterized by high protein concentrations that can be industrially valorized. Here, using an aqueous extraction scheme along with enzymatic proteolysis and FPLC (fast protein liquid chromatography)-based fractionation, a variety of hazelnut peptide fractions with varying bioactive properties were manufactured and their sequences were determined based on mass spectrometry. DPP-IV inhibitory attributes were determined based on an in vitro DPP-IV assay and in silico techniques were administered for for the analysis of overall bioactive potential and DPP-IV inhibitory characteristics of peptides. Based on these investigations, 256 peptides were identified in 81 different fractions. The majority of fractions were characterized with low to moderate DPP-IV inhibitory activity possibly due to their dilute nature. Some hazelnut peptides were characterized by comparable IC50 values as the positive control (Diprotin-A). The most influential 7 peptides were shown to generate higher docking scores than the control. The main interaction mechanism between hazelnut peptides and DPP-IV possibly depended on hydrophobic interactions. While further concentration could enhance the DPP-IV inhibitory potential of hazelnut peptides, hazelnut cakes represent a sustainable resource of potentially antidiabetic peptides. |
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