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Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition
Chitosan oligosaccharide (COS) is a bioactive compound derived from marine by-products. COS consumption has been demonstrated to lower the risk of diabetes. However, there are limited data on the inhibitory effect of low-molecular-weight COSs with different degrees of polymerization (DP) on α-glucos...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9740910/ https://www.ncbi.nlm.nih.gov/pubmed/36500221 http://dx.doi.org/10.3390/molecules27238129 |
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author | Khaisaat, Supharada Chancharoensin, Saovanee Wipatanawin, Angkana Suphantharika, Manop Payongsri, Panwajee |
author_facet | Khaisaat, Supharada Chancharoensin, Saovanee Wipatanawin, Angkana Suphantharika, Manop Payongsri, Panwajee |
author_sort | Khaisaat, Supharada |
collection | PubMed |
description | Chitosan oligosaccharide (COS) is a bioactive compound derived from marine by-products. COS consumption has been demonstrated to lower the risk of diabetes. However, there are limited data on the inhibitory effect of low-molecular-weight COSs with different degrees of polymerization (DP) on α-glucosidase. This study investigates the α-glucosidase inhibitory activity of two low-molecular-weight COSs, i.e., S-TU-COS with DP2–4 and L-TU-COS with DP2–5, both of which have different molecular weight distributions. The inhibition constants of the inhibitors binding to free enzymes (K(i)) and an enzyme–substrate complex (K(ii)) were investigated to elucidate the inhibitory mechanism of COSs with different chain lengths. The kinetic inhibition model of S-TU-COS showed non-completive inhibition results which are close to the uncompetitive inhibition results with K(i) and K(ii) values of 3.34 mM and 2.94 mM, respectively. In contrast, L-TU-COS showed uncompetitive inhibition with a K(ii) value of 5.84 mM. With this behavior, the IC(50) values of S-TU-COS and L-TU-COS decreased from 12.54 to 11.84 mM and 20.42 to 17.75 mM, respectively, with an increasing substrate concentration from 0.075 to 0.3 mM. This suggests that S-TU-COS is a more potent inhibitor, and the different DP of COS may cause significantly different inhibition (p < 0.05) on the α-glucosidase activity. This research may provide new insights into the production of a COS with a suitable profile for antidiabetic activity. |
format | Online Article Text |
id | pubmed-9740910 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-97409102022-12-11 Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition Khaisaat, Supharada Chancharoensin, Saovanee Wipatanawin, Angkana Suphantharika, Manop Payongsri, Panwajee Molecules Article Chitosan oligosaccharide (COS) is a bioactive compound derived from marine by-products. COS consumption has been demonstrated to lower the risk of diabetes. However, there are limited data on the inhibitory effect of low-molecular-weight COSs with different degrees of polymerization (DP) on α-glucosidase. This study investigates the α-glucosidase inhibitory activity of two low-molecular-weight COSs, i.e., S-TU-COS with DP2–4 and L-TU-COS with DP2–5, both of which have different molecular weight distributions. The inhibition constants of the inhibitors binding to free enzymes (K(i)) and an enzyme–substrate complex (K(ii)) were investigated to elucidate the inhibitory mechanism of COSs with different chain lengths. The kinetic inhibition model of S-TU-COS showed non-completive inhibition results which are close to the uncompetitive inhibition results with K(i) and K(ii) values of 3.34 mM and 2.94 mM, respectively. In contrast, L-TU-COS showed uncompetitive inhibition with a K(ii) value of 5.84 mM. With this behavior, the IC(50) values of S-TU-COS and L-TU-COS decreased from 12.54 to 11.84 mM and 20.42 to 17.75 mM, respectively, with an increasing substrate concentration from 0.075 to 0.3 mM. This suggests that S-TU-COS is a more potent inhibitor, and the different DP of COS may cause significantly different inhibition (p < 0.05) on the α-glucosidase activity. This research may provide new insights into the production of a COS with a suitable profile for antidiabetic activity. MDPI 2022-11-22 /pmc/articles/PMC9740910/ /pubmed/36500221 http://dx.doi.org/10.3390/molecules27238129 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 Khaisaat, Supharada Chancharoensin, Saovanee Wipatanawin, Angkana Suphantharika, Manop Payongsri, Panwajee Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition |
title | Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition |
title_full | Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition |
title_fullStr | Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition |
title_full_unstemmed | Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition |
title_short | Influence of Degree of Polymerization of Low-Molecular-Weight Chitosan Oligosaccharides on the α-Glucosidase Inhibition |
title_sort | influence of degree of polymerization of low-molecular-weight chitosan oligosaccharides on the α-glucosidase inhibition |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9740910/ https://www.ncbi.nlm.nih.gov/pubmed/36500221 http://dx.doi.org/10.3390/molecules27238129 |
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