Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein

The current study reported oat protein as a precursor for α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides and studied the antidiabetic activities related to their structures. Enzyme inhibition assays in vitro, using oat protein treated by alcalase and flavourzyme frac...

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Autores principales:	Lourdes Ramírez Fuentes, Caroline Richard, Lingyun Chen
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Oat protein Antidiabetic peptides Peptide sequencing α-amylase inhibition DPP-IV inhibition Type 2 diabetes Nutrition. Foods and food supply TX341-641
Acceso en línea:	https://doaj.org/article/7cee1d1bae804ae9ac467fc14cf73899
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spelling	oai:doaj.org-article:7cee1d1bae804ae9ac467fc14cf738992021-11-10T04:21:46ZSequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein1756-464610.1016/j.jff.2021.104829https://doaj.org/article/7cee1d1bae804ae9ac467fc14cf738992021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1756464621004783https://doaj.org/toc/1756-4646The current study reported oat protein as a precursor for α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides and studied the antidiabetic activities related to their structures. Enzyme inhibition assays in vitro, using oat protein treated by alcalase and flavourzyme fractionated into different molecular weights and hydrophobicity, indicated that the relatively hydrophobic fraction of 1–5 kDa inhibited enzymes related to glucose digestion, absorption, and metabolism activities. The α-amylase and DPP-IV were inhibited 57 and 78%, respectively, even at low peptide concentrations. LC-MS/MS analysis of the most effective fractions disclosed two eight amino acid sequences, identified from 12S oat globulin (GDVVALPA and DVVALPAG), and other sequences rich in amino acids like proline, leucine, valine, phenylalanine, and glutamine. The results suggest that proline and hydrophobic amino acids may favor hydrophobic interactions and hydrogen bonding with the target enzymes, especially the Leu-Pro sequence found in potent DPP-IV inhibitors.Lourdes Ramírez FuentesCaroline RichardLingyun ChenElsevierarticleOat proteinAntidiabetic peptidesPeptide sequencingα-amylase inhibitionDPP-IV inhibitionType 2 diabetesNutrition. Foods and food supplyTX341-641ENJournal of Functional Foods, Vol 87, Iss , Pp 104829- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Oat protein Antidiabetic peptides Peptide sequencing α-amylase inhibition DPP-IV inhibition Type 2 diabetes Nutrition. Foods and food supply TX341-641
spellingShingle	Oat protein Antidiabetic peptides Peptide sequencing α-amylase inhibition DPP-IV inhibition Type 2 diabetes Nutrition. Foods and food supply TX341-641 Lourdes Ramírez Fuentes Caroline Richard Lingyun Chen Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
description	The current study reported oat protein as a precursor for α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides and studied the antidiabetic activities related to their structures. Enzyme inhibition assays in vitro, using oat protein treated by alcalase and flavourzyme fractionated into different molecular weights and hydrophobicity, indicated that the relatively hydrophobic fraction of 1–5 kDa inhibited enzymes related to glucose digestion, absorption, and metabolism activities. The α-amylase and DPP-IV were inhibited 57 and 78%, respectively, even at low peptide concentrations. LC-MS/MS analysis of the most effective fractions disclosed two eight amino acid sequences, identified from 12S oat globulin (GDVVALPA and DVVALPAG), and other sequences rich in amino acids like proline, leucine, valine, phenylalanine, and glutamine. The results suggest that proline and hydrophobic amino acids may favor hydrophobic interactions and hydrogen bonding with the target enzymes, especially the Leu-Pro sequence found in potent DPP-IV inhibitors.
format	article
author	Lourdes Ramírez Fuentes Caroline Richard Lingyun Chen
author_facet	Lourdes Ramírez Fuentes Caroline Richard Lingyun Chen
author_sort	Lourdes Ramírez Fuentes
title	Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
title_short	Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
title_full	Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
title_fullStr	Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
title_full_unstemmed	Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein
title_sort	sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (dpp)-iv inhibitory peptides from oat protein
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/7cee1d1bae804ae9ac467fc14cf73899
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Sequential alcalase and flavourzyme treatment for preparation of α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory peptides from oat protein

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