Cargando…

Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions

Sericin, a byproduct of the silk industry, is an underutilized protein derived from the yellow silk cocoon. This research aimed to produce and characterize the bioactive peptides from sericin using various enzymatic hydrolysis methods. Alcalase, papain, neutrase, and protease were tested under their...

Descripción completa

Detalles Bibliográficos
Autores principales: Sangsawad, Papungkorn, Katemala, Sasikan, Pao, Danou, Suwanangul, Saranya, Jeencham, Rachasit, Sutheerawattananonda, Manote
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9741075/
https://www.ncbi.nlm.nih.gov/pubmed/36496739
http://dx.doi.org/10.3390/foods11233931
_version_ 1784848227961405440
author Sangsawad, Papungkorn
Katemala, Sasikan
Pao, Danou
Suwanangul, Saranya
Jeencham, Rachasit
Sutheerawattananonda, Manote
author_facet Sangsawad, Papungkorn
Katemala, Sasikan
Pao, Danou
Suwanangul, Saranya
Jeencham, Rachasit
Sutheerawattananonda, Manote
author_sort Sangsawad, Papungkorn
collection PubMed
description Sericin, a byproduct of the silk industry, is an underutilized protein derived from the yellow silk cocoon. This research aimed to produce and characterize the bioactive peptides from sericin using various enzymatic hydrolysis methods. Alcalase, papain, neutrase, and protease were tested under their respective digestion conditions. Among the enzymes tested, neutrase-catalyzed sericin into specific peptides with the strongest dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE) inhibitory properties. The peptides were subjected to a simulated in vitro gastrointestinal (GI) digestion in order to determine their stability. The GI peptides that were produced by neutrase hydrolysis continued to have the highest DPP-IV and ACE inhibitory activities. The neutrase -digested peptides were then fractionated via ultrafiltration; the peptide fraction with a molecular weight <3 kDa (UF3) inhibited DPP-IV and ACE activities. After being subjected to in vitro blood plasma hydrolysis, the UF3 was slightly degraded but retained its bioactivity. As a result of these findings, sericin peptides can be utilized as novel dietary ingredients that may alleviate some metabolic syndromes via the dual inhibitory properties of DPP-IV and ACE.
format Online
Article
Text
id pubmed-9741075
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-97410752022-12-11 Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions Sangsawad, Papungkorn Katemala, Sasikan Pao, Danou Suwanangul, Saranya Jeencham, Rachasit Sutheerawattananonda, Manote Foods Article Sericin, a byproduct of the silk industry, is an underutilized protein derived from the yellow silk cocoon. This research aimed to produce and characterize the bioactive peptides from sericin using various enzymatic hydrolysis methods. Alcalase, papain, neutrase, and protease were tested under their respective digestion conditions. Among the enzymes tested, neutrase-catalyzed sericin into specific peptides with the strongest dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE) inhibitory properties. The peptides were subjected to a simulated in vitro gastrointestinal (GI) digestion in order to determine their stability. The GI peptides that were produced by neutrase hydrolysis continued to have the highest DPP-IV and ACE inhibitory activities. The neutrase -digested peptides were then fractionated via ultrafiltration; the peptide fraction with a molecular weight <3 kDa (UF3) inhibited DPP-IV and ACE activities. After being subjected to in vitro blood plasma hydrolysis, the UF3 was slightly degraded but retained its bioactivity. As a result of these findings, sericin peptides can be utilized as novel dietary ingredients that may alleviate some metabolic syndromes via the dual inhibitory properties of DPP-IV and ACE. MDPI 2022-12-05 /pmc/articles/PMC9741075/ /pubmed/36496739 http://dx.doi.org/10.3390/foods11233931 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sangsawad, Papungkorn
Katemala, Sasikan
Pao, Danou
Suwanangul, Saranya
Jeencham, Rachasit
Sutheerawattananonda, Manote
Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions
title Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions
title_full Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions
title_fullStr Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions
title_full_unstemmed Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions
title_short Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions
title_sort integrated evaluation of dual-functional dpp-iv and ace inhibitory effects of peptides derived from sericin hydrolysis and their stabilities during in vitro-simulated gastrointestinal and plasmin digestions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9741075/
https://www.ncbi.nlm.nih.gov/pubmed/36496739
http://dx.doi.org/10.3390/foods11233931
work_keys_str_mv AT sangsawadpapungkorn integratedevaluationofdualfunctionaldppivandaceinhibitoryeffectsofpeptidesderivedfromsericinhydrolysisandtheirstabilitiesduringinvitrosimulatedgastrointestinalandplasmindigestions
AT katemalasasikan integratedevaluationofdualfunctionaldppivandaceinhibitoryeffectsofpeptidesderivedfromsericinhydrolysisandtheirstabilitiesduringinvitrosimulatedgastrointestinalandplasmindigestions
AT paodanou integratedevaluationofdualfunctionaldppivandaceinhibitoryeffectsofpeptidesderivedfromsericinhydrolysisandtheirstabilitiesduringinvitrosimulatedgastrointestinalandplasmindigestions
AT suwanangulsaranya integratedevaluationofdualfunctionaldppivandaceinhibitoryeffectsofpeptidesderivedfromsericinhydrolysisandtheirstabilitiesduringinvitrosimulatedgastrointestinalandplasmindigestions
AT jeenchamrachasit integratedevaluationofdualfunctionaldppivandaceinhibitoryeffectsofpeptidesderivedfromsericinhydrolysisandtheirstabilitiesduringinvitrosimulatedgastrointestinalandplasmindigestions
AT sutheerawattananondamanote integratedevaluationofdualfunctionaldppivandaceinhibitoryeffectsofpeptidesderivedfromsericinhydrolysisandtheirstabilitiesduringinvitrosimulatedgastrointestinalandplasmindigestions