Blue honeysuckle extracts retarded starch digestion by inhibiting glycosidases and changing the starch structure
Blue honeysuckle rich in anthocyanins can inhibit starch-digesting enzyme activity. This study evaluated the inhibitory effect and mechanism of blue honeysuckle extract (BHE) on glycosidases (α-amylase and α-glucosidase). BHE was a mixed glycosidase inhibitor with an IC 50 of 2.36 ± 0.14 and 0.06 ±...
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Veröffentlicht in: | Food & function 2022-06, Vol.13 (11), p.672-688 |
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creator | Zhang, Xinyue Rehman, Rizwan-ur Wang, Songxue Ji, Yanglin Li, Jing Liu, Suwen Wang, Hao |
description | Blue honeysuckle rich in anthocyanins can inhibit starch-digesting enzyme activity. This study evaluated the inhibitory effect and mechanism of blue honeysuckle extract (BHE) on glycosidases (α-amylase and α-glucosidase). BHE was a mixed glycosidase inhibitor with an IC
50
of 2.36 ± 0.14 and 0.06 ± 0.01 for α-amylase and α-glucosidase, respectively. Fourier transform infrared (FTIR) spectroscopy, multi-fluorescence spectroscopy, and isothermal titration calorimetry (ITC) confirmed that BHE caused the secondary structure change and static fluorescence quenching of glycosidases, and the interaction was an enthalpy-driven exothermic reaction. Molecular docking proved that the main anthocyanin monomers in BHE interacted with glycosidases through hydrogen bonds and van der Waals forces. Moreover, BHE changed the starch structure and prevented starch from being digested by glycosidases.
In vivo
, BHE and starch-BHE complexes effectively slowed postprandial hyperglycemia. This research provided a theoretical basis for BHE in antidiabetic healthy food research and development.
The effects and mechanism of blue honeysuckle extracts in inhibiting glycosidases and altering the starch structure were investigated in this study. |
doi_str_mv | 10.1039/d2fo00459c |
format | Article |
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50
of 2.36 ± 0.14 and 0.06 ± 0.01 for α-amylase and α-glucosidase, respectively. Fourier transform infrared (FTIR) spectroscopy, multi-fluorescence spectroscopy, and isothermal titration calorimetry (ITC) confirmed that BHE caused the secondary structure change and static fluorescence quenching of glycosidases, and the interaction was an enthalpy-driven exothermic reaction. Molecular docking proved that the main anthocyanin monomers in BHE interacted with glycosidases through hydrogen bonds and van der Waals forces. Moreover, BHE changed the starch structure and prevented starch from being digested by glycosidases.
In vivo
, BHE and starch-BHE complexes effectively slowed postprandial hyperglycemia. This research provided a theoretical basis for BHE in antidiabetic healthy food research and development.
The effects and mechanism of blue honeysuckle extracts in inhibiting glycosidases and altering the starch structure were investigated in this study.</description><identifier>ISSN: 2042-6496</identifier><identifier>EISSN: 2042-650X</identifier><identifier>DOI: 10.1039/d2fo00459c</identifier><identifier>PMID: 35550649</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Amylases ; Anthocyanins ; Calorimetry ; Diabetes mellitus ; Digestion ; Enthalpy ; Enzymatic activity ; Enzyme activity ; Exothermic reactions ; Fluorescence ; Fluorescence spectroscopy ; Fourier transforms ; Glucosidase ; Glycosidases ; Hydrogen bonding ; Hydrogen bonds ; Hyperglycemia ; Infrared spectroscopy ; Molecular docking ; Monomers ; Protein structure ; R&D ; Research & development ; Secondary structure ; Spectroscopy ; Starch ; Titration ; Titration calorimetry ; Van der Waals forces ; α-Amylase ; α-Glucosidase</subject><ispartof>Food & function, 2022-06, Vol.13 (11), p.672-688</ispartof><rights>Copyright Royal Society of Chemistry 2022</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c252t-4413467edb9e581e1da87b1d6372cee77440e6fed1123a2f98bc21b710d587703</citedby><cites>FETCH-LOGICAL-c252t-4413467edb9e581e1da87b1d6372cee77440e6fed1123a2f98bc21b710d587703</cites><orcidid>0000-0001-6506-4847 ; 0000-0001-9273-1801</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35550649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Xinyue</creatorcontrib><creatorcontrib>Rehman, Rizwan-ur</creatorcontrib><creatorcontrib>Wang, Songxue</creatorcontrib><creatorcontrib>Ji, Yanglin</creatorcontrib><creatorcontrib>Li, Jing</creatorcontrib><creatorcontrib>Liu, Suwen</creatorcontrib><creatorcontrib>Wang, Hao</creatorcontrib><title>Blue honeysuckle extracts retarded starch digestion by inhibiting glycosidases and changing the starch structure</title><title>Food & function</title><addtitle>Food Funct</addtitle><description>Blue honeysuckle rich in anthocyanins can inhibit starch-digesting enzyme activity. This study evaluated the inhibitory effect and mechanism of blue honeysuckle extract (BHE) on glycosidases (α-amylase and α-glucosidase). BHE was a mixed glycosidase inhibitor with an IC
50
of 2.36 ± 0.14 and 0.06 ± 0.01 for α-amylase and α-glucosidase, respectively. Fourier transform infrared (FTIR) spectroscopy, multi-fluorescence spectroscopy, and isothermal titration calorimetry (ITC) confirmed that BHE caused the secondary structure change and static fluorescence quenching of glycosidases, and the interaction was an enthalpy-driven exothermic reaction. Molecular docking proved that the main anthocyanin monomers in BHE interacted with glycosidases through hydrogen bonds and van der Waals forces. Moreover, BHE changed the starch structure and prevented starch from being digested by glycosidases.
In vivo
, BHE and starch-BHE complexes effectively slowed postprandial hyperglycemia. This research provided a theoretical basis for BHE in antidiabetic healthy food research and development.
The effects and mechanism of blue honeysuckle extracts in inhibiting glycosidases and altering the starch structure were investigated in this study.</description><subject>Amylases</subject><subject>Anthocyanins</subject><subject>Calorimetry</subject><subject>Diabetes mellitus</subject><subject>Digestion</subject><subject>Enthalpy</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Exothermic reactions</subject><subject>Fluorescence</subject><subject>Fluorescence spectroscopy</subject><subject>Fourier transforms</subject><subject>Glucosidase</subject><subject>Glycosidases</subject><subject>Hydrogen bonding</subject><subject>Hydrogen bonds</subject><subject>Hyperglycemia</subject><subject>Infrared spectroscopy</subject><subject>Molecular docking</subject><subject>Monomers</subject><subject>Protein structure</subject><subject>R&D</subject><subject>Research & development</subject><subject>Secondary structure</subject><subject>Spectroscopy</subject><subject>Starch</subject><subject>Titration</subject><subject>Titration calorimetry</subject><subject>Van der Waals forces</subject><subject>α-Amylase</subject><subject>α-Glucosidase</subject><issn>2042-6496</issn><issn>2042-650X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNpdkc1LJDEQxYO4qLhevCsBL4swu_nsdI466xcMzGUFb006qZ6O9nSPSRqc_34zjqNgXarg_ap41EPolJLflHD9x7FmIERIbffQESOCTQpJnvZ3s9DFITqJ8Znk4lqXujxAh1xKSbJ2hFbX3Qi4HXpYx9G-dIDhLQVjU8QBkgkOHI652xY7v4CY_NDjeo193_raJ98v8KJb2yF6ZyJEbHqHbWv6xUZJLeyWYwqjTWOAn-hHY7oIJx_9GD3e3vyb3k9m87uH6dVsYplkaSIE5aJQ4GoNsqRAnSlVTV3BFbMASglBoGjAUcq4YY0ua8torShxslSK8GP0a3t3FYbXMRuvlj5a6DrTwzDGihWFUKUUpMzoxTf0eRhDn91lSvHsg-sNdbmlbBhiDNBUq-CXJqwrSqpNFNVfdjt_j2Ka4fOPk2O9BPeJ7h6fgbMtEKL9VL-y5P8BUPKOuA</recordid><startdate>20220606</startdate><enddate>20220606</enddate><creator>Zhang, Xinyue</creator><creator>Rehman, Rizwan-ur</creator><creator>Wang, Songxue</creator><creator>Ji, Yanglin</creator><creator>Li, Jing</creator><creator>Liu, Suwen</creator><creator>Wang, Hao</creator><general>Royal Society of Chemistry</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>7T7</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6506-4847</orcidid><orcidid>https://orcid.org/0000-0001-9273-1801</orcidid></search><sort><creationdate>20220606</creationdate><title>Blue honeysuckle extracts retarded starch digestion by inhibiting glycosidases and changing the starch structure</title><author>Zhang, Xinyue ; Rehman, Rizwan-ur ; Wang, Songxue ; Ji, Yanglin ; Li, Jing ; Liu, Suwen ; Wang, Hao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c252t-4413467edb9e581e1da87b1d6372cee77440e6fed1123a2f98bc21b710d587703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Amylases</topic><topic>Anthocyanins</topic><topic>Calorimetry</topic><topic>Diabetes mellitus</topic><topic>Digestion</topic><topic>Enthalpy</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Exothermic reactions</topic><topic>Fluorescence</topic><topic>Fluorescence spectroscopy</topic><topic>Fourier transforms</topic><topic>Glucosidase</topic><topic>Glycosidases</topic><topic>Hydrogen bonding</topic><topic>Hydrogen bonds</topic><topic>Hyperglycemia</topic><topic>Infrared spectroscopy</topic><topic>Molecular docking</topic><topic>Monomers</topic><topic>Protein structure</topic><topic>R&D</topic><topic>Research & development</topic><topic>Secondary structure</topic><topic>Spectroscopy</topic><topic>Starch</topic><topic>Titration</topic><topic>Titration calorimetry</topic><topic>Van der Waals forces</topic><topic>α-Amylase</topic><topic>α-Glucosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Xinyue</creatorcontrib><creatorcontrib>Rehman, Rizwan-ur</creatorcontrib><creatorcontrib>Wang, Songxue</creatorcontrib><creatorcontrib>Ji, Yanglin</creatorcontrib><creatorcontrib>Li, Jing</creatorcontrib><creatorcontrib>Liu, Suwen</creatorcontrib><creatorcontrib>Wang, Hao</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Food & function</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Xinyue</au><au>Rehman, Rizwan-ur</au><au>Wang, Songxue</au><au>Ji, Yanglin</au><au>Li, Jing</au><au>Liu, Suwen</au><au>Wang, Hao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Blue honeysuckle extracts retarded starch digestion by inhibiting glycosidases and changing the starch structure</atitle><jtitle>Food & function</jtitle><addtitle>Food Funct</addtitle><date>2022-06-06</date><risdate>2022</risdate><volume>13</volume><issue>11</issue><spage>672</spage><epage>688</epage><pages>672-688</pages><issn>2042-6496</issn><eissn>2042-650X</eissn><abstract>Blue honeysuckle rich in anthocyanins can inhibit starch-digesting enzyme activity. This study evaluated the inhibitory effect and mechanism of blue honeysuckle extract (BHE) on glycosidases (α-amylase and α-glucosidase). BHE was a mixed glycosidase inhibitor with an IC
50
of 2.36 ± 0.14 and 0.06 ± 0.01 for α-amylase and α-glucosidase, respectively. Fourier transform infrared (FTIR) spectroscopy, multi-fluorescence spectroscopy, and isothermal titration calorimetry (ITC) confirmed that BHE caused the secondary structure change and static fluorescence quenching of glycosidases, and the interaction was an enthalpy-driven exothermic reaction. Molecular docking proved that the main anthocyanin monomers in BHE interacted with glycosidases through hydrogen bonds and van der Waals forces. Moreover, BHE changed the starch structure and prevented starch from being digested by glycosidases.
In vivo
, BHE and starch-BHE complexes effectively slowed postprandial hyperglycemia. This research provided a theoretical basis for BHE in antidiabetic healthy food research and development.
The effects and mechanism of blue honeysuckle extracts in inhibiting glycosidases and altering the starch structure were investigated in this study.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>35550649</pmid><doi>10.1039/d2fo00459c</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0001-6506-4847</orcidid><orcidid>https://orcid.org/0000-0001-9273-1801</orcidid></addata></record> |
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subjects | Amylases Anthocyanins Calorimetry Diabetes mellitus Digestion Enthalpy Enzymatic activity Enzyme activity Exothermic reactions Fluorescence Fluorescence spectroscopy Fourier transforms Glucosidase Glycosidases Hydrogen bonding Hydrogen bonds Hyperglycemia Infrared spectroscopy Molecular docking Monomers Protein structure R&D Research & development Secondary structure Spectroscopy Starch Titration Titration calorimetry Van der Waals forces α-Amylase α-Glucosidase |
title | Blue honeysuckle extracts retarded starch digestion by inhibiting glycosidases and changing the starch structure |
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