Glucoregulatory Properties of a Protein Hydrolysate from Atlantic Salmon ( Salmo salar ): Preliminary Characterization and Evaluation of DPP-IV Inhibition and Direct Glucose Uptake In Vitro

Metabolic disorders are increasingly prevalent conditions that manifest pathophysiologically along a continuum. Among reported metabolic risk factors, elevated fasting serum glucose (FSG) levels have shown the most substantial increase in risk exposure. Ultimately leading to insulin resistance (IR),...

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Bibliographic Details
Published in:Marine Drugs
Main Authors: Christian Bjerknes, Sileshi Gizachew Wubshet, Sissel Beate Rønning, Nils Kristian Afseth, Crawford Currie, Bomi Framroze, Erland Hermansen
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2024
Subjects:
marine protein hydrolysate
DPP-IV inhibition
glucose uptake
glucoregulatory peptides
bioactive peptides
salmon protein hydrolysate
Biology (General)
QH301-705.5
Atlantic salmon
Salmo salar
Online Access:https://doi.org/10.3390/md22040151
https://doaj.org/article/5c39946ff5e749629d0b21e3f3faa638
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Summary:Metabolic disorders are increasingly prevalent conditions that manifest pathophysiologically along a continuum. Among reported metabolic risk factors, elevated fasting serum glucose (FSG) levels have shown the most substantial increase in risk exposure. Ultimately leading to insulin resistance (IR), this condition is associated with notable deteriorations in the prognostic outlook for major diseases, including neurodegenerative diseases, cancer risk, and mortality related to cardiovascular disease. Tackling metabolic dysfunction, with a focus on prevention, is a critically important aspect for human health. In this study, an investigation into the potential antidiabetic properties of a salmon protein hydrolysate (SPH) was conducted, focusing on its potential dipeptidyl peptidase-IV (DPP-IV) inhibition and direct glucose uptake in vitro. Characterization of the SPH utilized a bioassay-guided fractionation approach to identify potent glucoregulatory peptide fractions. Low-molecular-weight (MW) fractions prepared by membrane filtration (MWCO = 3 kDa) showed significant DPP-IV inhibition (IC 50 = 1.01 ± 0.12 mg/mL) and glucose uptake in vitro ( p ≤ 0.0001 at 1 mg/mL). Further fractionation of the lowest MW fractions (<3 kDa) derived from the permeate resulted in three peptide subfractions. The subfraction with the lowest molecular weight demonstrated the most significant glucose uptake activity ( p ≤ 0.0001), maintaining its potency even at a dilution of 1:500 ( p ≤ 0.01).

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