Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions
Phenolic acids are involved in modulating the activity of starch digestive enzymes but remains unclear if their interaction with enzymes or starch is governing the inhibition. The potential inhibition of nine phenolic acids against α-amylase and α-glucosidase was studied applying different methodologies to understand interactions between phenolic acids and either enzymes or substrates. Vanillic and syringic acids were prone to interact with α-amylase requiring low half-maximum inhibitory concentration (IC50) to inhibit starch hydrolysis. Nevertheless, the initial interaction of phenolic acids with starch somewhat obstructed their interaction with starch, requiring 10 times higher IC50, with the exception of chlorogenic and gallic acid. The study demonstrates that 10% of the phenolic acids were retained during starch gelatinization. Those effects were not really evident with α-glucosidase, likely due to the small molecular size of maltose substrate. Phenolic acids with > 1 hydroxyl group like caffeic and protocatechuic acids showed the lowest IC50 against α-glucosidase.
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Format: | artículo biblioteca |
Language: | English |
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Elsevier
2021-09-27
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Subjects: | Digestive enzymes, Starch, Gelatinization, Maltose, In vitro reaction, |
Online Access: | http://hdl.handle.net/10261/253598 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100004837 |
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dig-iata-es-10261-2535982022-07-01T10:45:09Z Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions Aleixandre, Andrea Gil, José Vicente Sineiro, Jorge Rosell, Cristina M. Ministerio de Ciencia e Innovación (España) Generalitat Valenciana European Commission Digestive enzymes Starch Gelatinization Maltose In vitro reaction Phenolic acids are involved in modulating the activity of starch digestive enzymes but remains unclear if their interaction with enzymes or starch is governing the inhibition. The potential inhibition of nine phenolic acids against α-amylase and α-glucosidase was studied applying different methodologies to understand interactions between phenolic acids and either enzymes or substrates. Vanillic and syringic acids were prone to interact with α-amylase requiring low half-maximum inhibitory concentration (IC50) to inhibit starch hydrolysis. Nevertheless, the initial interaction of phenolic acids with starch somewhat obstructed their interaction with starch, requiring 10 times higher IC50, with the exception of chlorogenic and gallic acid. The study demonstrates that 10% of the phenolic acids were retained during starch gelatinization. Those effects were not really evident with α-glucosidase, likely due to the small molecular size of maltose substrate. Phenolic acids with > 1 hydroxyl group like caffeic and protocatechuic acids showed the lowest IC50 against α-glucosidase. Financial support of the Spanish Ministry of Science and Innovation (Project RTI2018-095919-B-C21, Project RTI2018-095919-B-C22) and the European Regional Development Fund (FEDER) and Generalitat Valenciana (Project Prometeo 2017/189). Peer reviewed 2021-11-04T06:48:21Z 2021-11-04T06:48:21Z 2021-09-27 artículo http://purl.org/coar/resource_type/c_6501 Food Chemistry 372: 131231 (2022) 0308-8146 http://hdl.handle.net/10261/253598 10.1016/j.foodchem.2021.131231 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100004837 en #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-095919-B-C21 info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-095919-B-C22 Publisher's version https://doi.org/10.1016/j.foodchem.2021.131231 Sí open Elsevier |
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Digestive enzymes Starch Gelatinization Maltose In vitro reaction Digestive enzymes Starch Gelatinization Maltose In vitro reaction |
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Digestive enzymes Starch Gelatinization Maltose In vitro reaction Digestive enzymes Starch Gelatinization Maltose In vitro reaction Aleixandre, Andrea Gil, José Vicente Sineiro, Jorge Rosell, Cristina M. Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions |
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Phenolic acids are involved in modulating the activity of starch digestive enzymes but remains unclear if their interaction with enzymes or starch is governing the inhibition. The potential inhibition of nine phenolic acids against α-amylase and α-glucosidase was studied applying different methodologies to understand interactions between phenolic acids and either enzymes or substrates. Vanillic and syringic acids were prone to interact with α-amylase requiring low half-maximum inhibitory concentration (IC50) to inhibit starch hydrolysis. Nevertheless, the initial interaction of phenolic acids with starch somewhat obstructed their interaction with starch, requiring 10 times higher IC50, with the exception of chlorogenic and gallic acid. The study demonstrates that 10% of the phenolic acids were retained during starch gelatinization. Those effects were not really evident with α-glucosidase, likely due to the small molecular size of maltose substrate. Phenolic acids with > 1 hydroxyl group like caffeic and protocatechuic acids showed the lowest IC50 against α-glucosidase. |
author2 |
Ministerio de Ciencia e Innovación (España) |
author_facet |
Ministerio de Ciencia e Innovación (España) Aleixandre, Andrea Gil, José Vicente Sineiro, Jorge Rosell, Cristina M. |
format |
artículo |
topic_facet |
Digestive enzymes Starch Gelatinization Maltose In vitro reaction |
author |
Aleixandre, Andrea Gil, José Vicente Sineiro, Jorge Rosell, Cristina M. |
author_sort |
Aleixandre, Andrea |
title |
Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions |
title_short |
Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions |
title_full |
Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions |
title_fullStr |
Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions |
title_full_unstemmed |
Understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions |
title_sort |
understanding phenolic acids inhibition of α-amylase and α-glucosidase and influence of reaction conditions |
publisher |
Elsevier |
publishDate |
2021-09-27 |
url |
http://hdl.handle.net/10261/253598 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100004837 |
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