DPP-IV Inhibitory Peptides GPF, IGL, and GGGW Obtained from Chicken Blood Hydrolysates

Autor: Fidel Toldrá, Gisela Carrera Alvarado, Leticia Mora Soler
Přispěvatelé: Ministerio de Ciencia e Innovación (España), Generalitat Valenciana
Rok vydání: 2022
Předmět:
Zdroj: International Journal of Molecular Sciences; Volume 23; Issue 22; Pages: 14140
ISSN: 1422-0067
DOI: 10.3390/ijms232214140
Popis: Blood is a meat by-product rich in proteins with properties that can be improved after hydrolysis, making it a sustainable alternative for use in the generation of bioactive peptides. The objective of this study was to identify dipeptidyl peptidase IV (DPP-IV) inhibitory peptides obtained from different chicken blood hydrolysates prepared using combinations of four different enzymes. Best results were observed for AP (2% Alcalase + 5% Protana Prime) and APP (2% Alcalase + 5% Protana Prime + 3% Protana UBoost) hydrolysates obtaining inhibition values of 60.55 and 53.61%, respectively, assayed at a concentration of 10 mg/mL. Free amino acids were determined to establish the impact of exopeptidase activity in the samples. A total of 79 and 12 sequences of peptides were identified by liquid chromatography and mass spectrometry in tandem (LC-MS/MS) in AP and APP samples, respectively. Nine of the identified peptides were established as potential DPP-IV inhibitory using in silico approaches and later synthesized for confirmation. Thus, peptides GPF, IGL, and GGGW showed good DPP-IV inhibitory activity with IC50 values of 0.94, 2.22, and 2.73 mM, respectively. This study confirmed the potential of peptides obtained from chicken blood hydrolysates to be used as DPP-IV inhibitors and, therefore, in the control or modulation of type 2 diabetes.
This research was funded by Grant PID2020-119684RB-I00 funded by MCIN/AEI/10.13039/501100011033. Grant GRISOLIAP/2020/021 de la Consellería de Innovació, Universitats, Ciència i Societat Digital de la Generalitat Valenciana (GCA) is also acknowledged. The proteomic analysis was performed in the proteomics facility of SCSIE University of Valencia that belongs to Proteored.
Databáze: OpenAIRE
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