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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Main Authors: Ahmet Furkan Çağlar, Ayşe Gülden Göksu, Bilal Çakır, İbrahim Gülseren
Format: Article
Language:English
Published: Elsevier 2021-12-01
Series:Food Chemistry: X
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2590157521000390
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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
collection DOAJ
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.
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spelling doaj.art-29f649acecc64ed9ada69a13532f39242022-12-21T19:33:55ZengElsevierFood Chemistry: X2590-15752021-12-0112100151Tombul hazelnut (Corylus avellana L.) peptides with DPP-IV inhibitory activity: In vitro and in silico studiesAhmet Furkan Çağlar0Ayşe Gülden Göksu1Bilal Çakır2İbrahim Gülseren3Department of Food Engineering, İstanbul S. Zaim University (İZÜ), Halkalı – Küçükçekmece, İstanbul, TurkeyDepartment of Food Engineering, İstanbul S. Zaim University (İZÜ), Halkalı – Küçükçekmece, İstanbul, Turkeyİstanbul S. Zaim University (İZÜ), Halal Food R&D Center, Halkalı, Küçükçekmece, İstanbul, Turkey; İZÜ Food and Agricultural Research Center (GTÜAM), Halkalı Campus, 34303 Küçükçekmece, İstanbul, Turkey; Corresponding author at: İstanbul S. Zaim University (İZÜ), Halal Food R&D Center, Halkalı, Küçükçekmece, İstanbul, Turkey.Department of Food Engineering, İstanbul S. Zaim University (İZÜ), Halkalı – Küçükçekmece, İstanbul, Turkey; İZÜ Food and Agricultural Research Center (GTÜAM), Halkalı Campus, 34303 Küçükçekmece, İstanbul, TurkeyCold 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.http://www.sciencedirect.com/science/article/pii/S2590157521000390Hazelnut proteinsValorizationBioactive peptidesAntidiabetic activityMolecular docking
spellingShingle 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
Food Chemistry: X
Hazelnut proteins
Valorization
Bioactive peptides
Antidiabetic activity
Molecular docking
title 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_short 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
topic Hazelnut proteins
Valorization
Bioactive peptides
Antidiabetic activity
Molecular docking
url http://www.sciencedirect.com/science/article/pii/S2590157521000390
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