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Sequence alterations affect the antidiabetic attributes of hazelnut peptide fractions during the industrial manufacture and simulated digestion of hazelnut paste

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Abstract

Press cakes are by-products of cold press oil manufacture and are characterized by significant protein concentrations. Our group has previously demonstrated potential bioactive attributes of hazelnut protein hydrolysates including their antidiabetic activities. Here, an effort was made to utilize DPP-IV (Dipeptidyl peptidase-IV)-inhibitory hazelnut peptides in industrial food manufacture. Hazelnut protein isolates (approx. 95% protein) were obtained via an alkali extraction-isoelectric precipitation method. Papain, bromelain and pepsin were used in the enzymatic hydrolysis and hydrolysates were fractionated via Fast Protein Liquid Chromatography. As a general observation, although fractionation lead to dilution of the samples, fractions were observed to be more bioactive than the total hydrolysates. In vitro antidiabetic activities of the fractions were tested and 3 antidiabetic fractions were added to hazelnut paste. Afterwards simulated gastrointestinal digestion and antidiabetic activity assays were performed. DPP-IV inhibition was the major antidiabetic mechanism in the fractions and digested paste, while some fractions were characterized by comparable IC50 values as the positive controls. Alpha-glucosidase inhibition was limited by digestion trials, whereas alpha-amylase inhibition was only slight in the digested paste (< %6). In silico analyses predicted partial degradation of the peptides, whereas the interactions between DPP-IV or alpha-glucosidase and hazelnut peptides were predicted to be significant (p < 0.05). Consequently hazelnut press cakes were regarded as a potential source of antidiabetic peptides that can be used in industrial manufacture of functional foods, while food processing conditions or gastrointestinal digestion could largely affect peptide bioactivity.

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Abbreviations

AE-IP:

Alkali extraction-isoelectric precipitation

DEAE:

Diethylaminoethyl

DNS:

3,5-Dinitrosalicylic acid

DPP-IV:

Dipeptidyl peptidase-IV

FPLC:

Fast protein liquid chromatography

GLP-1:

Glucagon-like peptide-1

IC50 :

Half maximal inhibitory concentration

LC-Q-TOF/MS:

Liquid chromatography quadrupole time-of-flight mass spectrometry

pNA:

p-nitroanilide

pNPG:

p-nitrophenyl glucopyranoside

PVDF:

Polyvinylidene

SGF:

Simulated gastric fluid

SIF:

Simulated intestinal fluid

SSF:

Simulated salivary fluid

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Acknowledgements

Hazelnut cakes were donated by Neva Foods. The authors would like to thank Prof. Dr. Ahmet Tarık Baykal and Ms. Emel Akgün for their technical support at Labmed. The industrial manufacture was possible due to the support of FİSKOBİRLİK, Giresun, Turkey.

Funding

This study was funded by a grant from The Scientific and Technological Research Council of Turkey (TÜBİTAK) 1001 Program, Turkey (Grant No. 217O063).

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AGG: Methodology; Validation; Formal analysis; Investigation; Data Curation; Writing—Original Draft; Visualization. BÇ: Conceptualization; Methodology; Formal analysis; Supervision; Funding acquisition. İG Conceptualization; Methodology; Resources; Data Curation; Writing—Review & Editing; Supervision; Project administration; Funding acquisition.

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Correspondence to İbrahim Gülseren.

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Göksu, A.G., Çakır, B. & Gülseren, İ. Sequence alterations affect the antidiabetic attributes of hazelnut peptide fractions during the industrial manufacture and simulated digestion of hazelnut paste. J Food Sci Technol 60, 171–180 (2023). https://doi.org/10.1007/s13197-022-05601-2

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