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:	Ahmet Furkan Çağlar, Ayşe Gülden Göksu, Bilal Çakır, İbrahim Gülseren
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Hazelnut proteins Valorization Bioactive peptides Antidiabetic activity Molecular docking Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
Acceso en línea:	https://doaj.org/article/29f649acecc64ed9ada69a13532f3924
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spelling	oai:doaj.org-article:29f649acecc64ed9ada69a13532f39242021-11-28T04:37:46ZTombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies2590-157510.1016/j.fochx.2021.100151https://doaj.org/article/29f649acecc64ed9ada69a13532f39242021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2590157521000390https://doaj.org/toc/2590-1575Cold 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.Ahmet Furkan ÇağlarAyşe Gülden GöksuBilal Çakırİbrahim GülserenElsevierarticleHazelnut proteinsValorizationBioactive peptidesAntidiabetic activityMolecular dockingNutrition. Foods and food supplyTX341-641Food processing and manufactureTP368-456ENFood Chemistry: X, Vol 12, Iss , Pp 100151- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Hazelnut proteins Valorization Bioactive peptides Antidiabetic activity Molecular docking Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456
spellingShingle	Hazelnut proteins Valorization Bioactive peptides Antidiabetic activity Molecular docking Nutrition. Foods and food supply TX341-641 Food processing and manufacture TP368-456 Ahmet Furkan Çağlar Ayşe Gülden Göksu Bilal Çakır İbrahim Gülseren Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies
description	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.
format	article
author	Ahmet Furkan Çağlar Ayşe Gülden Göksu Bilal Çakır İbrahim Gülseren
author_facet	Ahmet Furkan Çağlar Ayşe Gülden Göksu Bilal Çakır İbrahim Gülseren
author_sort	Ahmet Furkan Çağlar
title	Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies
title_short	Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies
title_full	Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies
title_fullStr	Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies
title_full_unstemmed	Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies
title_sort	tombul hazelnut (corylus avellana l.) peptides with dpp-iv inhibitory activity: in vitro and in silico studies
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/29f649acecc64ed9ada69a13532f3924
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Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studies

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