Enzymic catalyzing affinity to substrate affects inhibitor-enzyme binding interactions: Inhibition behaviors of EGCG against starch digestion by individual and co-existing α-amylase and amyloglucosidase
•Epigallocatechin gallate(EGCG) inhibits amylase(AA) at slowly-digestible-starch phase.•EGCG inhibited amyloglucosidase(AMG) and AA/AMG in the whole digestion process.•Binding of EGCG with AA and AMG causes more unbound AMG in AA/AMG system.•Although EGCG-AA binding affinity was higher than EGCG-AMG...
Gespeichert in:
| Veröffentlicht in: | Food chemistry 2022-09, Vol.388, p.133047-133047, Article 133047 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 133047 |
|---|---|
| container_issue | |
| container_start_page | 133047 |
| container_title | Food chemistry |
| container_volume | 388 |
| creator | Zhu, Shengnan Li, Jing Li, Wenyue Li, Shuangshuang Yang, Xi Liu, Xuebo Sun, Lijun |
| description | •Epigallocatechin gallate(EGCG) inhibits amylase(AA) at slowly-digestible-starch phase.•EGCG inhibited amyloglucosidase(AMG) and AA/AMG in the whole digestion process.•Binding of EGCG with AA and AMG causes more unbound AMG in AA/AMG system.•Although EGCG-AA binding affinity was higher than EGCG-AMG, AA inhibition was weaker.•High catalytic affinity of AA to starch weakens EGCG-AA binding in digestion system.
The inhibition of (-)-epigallocatechin-gallate (EGCG) against starch digestion by α-amylase (AA), amyloglucosidase (AMG) and co-existing enzymes (AA/AMG) were comparatively studied. EGCG inhibited AA only at slowly-digestible-starch (SDS) phase. This resulted from high catalytic efficiency of AA for rapidly-digestible-starch (RDS), counteracting the inhibition at this phase. EGCG inhibited AMG and AA/AMG during whole process. At RDS phase, the catalytic velocity of AMG was always higher than AA/AMG because of an antagonistic effect of two enzymes. However, at SDS phase with EGCG, the catalytic velocity of AA/AMG was higher than AMG. This is because binding of EGCG with both enzymes caused more unbound AMG that generated more glucose in co-existing AA/AMG than AMG. Although EGCG-AA binding affinity was higher than EGCG-AMG, competitive inhibition of EGCG against AA was weaker than AMG, indicating relatively higher binding/catalyzing affinity of AA to starch significantly weakened EGCG-AA binding due to competitive relationship between starch and EGCG. |
| doi_str_mv | 10.1016/j.foodchem.2022.133047 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2658229655</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0308814622010093</els_id><sourcerecordid>2658229655</sourcerecordid><originalsourceid>FETCH-LOGICAL-c283t-6d43712b1abe5ebfe4779ad31fc23c1bb4c88cdd7b86a28d7f858aa428178af73</originalsourceid><addsrcrecordid>eNqFkc2O0zAUhSMEYsrAK4y8ZJPinyR2WYGqUkYaiQ2sLf_ctLdK4sF2KjpvxXMg8UwkZIYtK9v3nnPPtb6iuGF0zShr3p3WbQjeHaFfc8r5mglBK_msWDElRSmp5M-LFRVUlYpVzVXxKqUTpZRTpl4WV6KulOAbuip-7YaHS4-OOJNNd3nA4UBM2-KA-UJyIGm0KUeTYa6Cy4ngcESLOcQSZisQi4OfbThkiMZlDEN6T24X2fQgFo7mjCEmElqy22_3xBwMDimTlE10R-LxAGmRXsg87Yx-NB0xgyculPADp-6U8PtnafpLZxL8bc33cOhGFxL6qfi6eNGaLsGbx_O6-PZp93X7ubz7sr_dfrwrHVcil42vhGTcMmOhBttCJeXGeMFax4Vj1lZOKee9tKoxXHnZqloZU3HFpDKtFNfF22XufQzfx2lz3WNy0HVmgDAmzZtacb5p6nqSNovUxZBShFbfR-xNvGhG9QxSn_QTSD2D1AvIyXjzmDHaHvw_2xO5SfBhEcD00zNC1MkhDA48xomT9gH_l_EH93m6GA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2658229655</pqid></control><display><type>article</type><title>Enzymic catalyzing affinity to substrate affects inhibitor-enzyme binding interactions: Inhibition behaviors of EGCG against starch digestion by individual and co-existing α-amylase and amyloglucosidase</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Zhu, Shengnan ; Li, Jing ; Li, Wenyue ; Li, Shuangshuang ; Yang, Xi ; Liu, Xuebo ; Sun, Lijun</creator><creatorcontrib>Zhu, Shengnan ; Li, Jing ; Li, Wenyue ; Li, Shuangshuang ; Yang, Xi ; Liu, Xuebo ; Sun, Lijun</creatorcontrib><description>•Epigallocatechin gallate(EGCG) inhibits amylase(AA) at slowly-digestible-starch phase.•EGCG inhibited amyloglucosidase(AMG) and AA/AMG in the whole digestion process.•Binding of EGCG with AA and AMG causes more unbound AMG in AA/AMG system.•Although EGCG-AA binding affinity was higher than EGCG-AMG, AA inhibition was weaker.•High catalytic affinity of AA to starch weakens EGCG-AA binding in digestion system.
The inhibition of (-)-epigallocatechin-gallate (EGCG) against starch digestion by α-amylase (AA), amyloglucosidase (AMG) and co-existing enzymes (AA/AMG) were comparatively studied. EGCG inhibited AA only at slowly-digestible-starch (SDS) phase. This resulted from high catalytic efficiency of AA for rapidly-digestible-starch (RDS), counteracting the inhibition at this phase. EGCG inhibited AMG and AA/AMG during whole process. At RDS phase, the catalytic velocity of AMG was always higher than AA/AMG because of an antagonistic effect of two enzymes. However, at SDS phase with EGCG, the catalytic velocity of AA/AMG was higher than AMG. This is because binding of EGCG with both enzymes caused more unbound AMG that generated more glucose in co-existing AA/AMG than AMG. Although EGCG-AA binding affinity was higher than EGCG-AMG, competitive inhibition of EGCG against AA was weaker than AMG, indicating relatively higher binding/catalyzing affinity of AA to starch significantly weakened EGCG-AA binding due to competitive relationship between starch and EGCG.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2022.133047</identifier><identifier>PMID: 35483290</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>alpha-Amylases - metabolism ; Amylases ; Amyloglucosidase ; Binding interactions ; Co-existing enzymes ; Digestion ; EGCG ; Glucan 1,4-alpha-Glucosidase - metabolism ; Starch - metabolism ; α-Amylase</subject><ispartof>Food chemistry, 2022-09, Vol.388, p.133047-133047, Article 133047</ispartof><rights>2022 Elsevier Ltd</rights><rights>Copyright © 2022 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c283t-6d43712b1abe5ebfe4779ad31fc23c1bb4c88cdd7b86a28d7f858aa428178af73</citedby><cites>FETCH-LOGICAL-c283t-6d43712b1abe5ebfe4779ad31fc23c1bb4c88cdd7b86a28d7f858aa428178af73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0308814622010093$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35483290$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhu, Shengnan</creatorcontrib><creatorcontrib>Li, Jing</creatorcontrib><creatorcontrib>Li, Wenyue</creatorcontrib><creatorcontrib>Li, Shuangshuang</creatorcontrib><creatorcontrib>Yang, Xi</creatorcontrib><creatorcontrib>Liu, Xuebo</creatorcontrib><creatorcontrib>Sun, Lijun</creatorcontrib><title>Enzymic catalyzing affinity to substrate affects inhibitor-enzyme binding interactions: Inhibition behaviors of EGCG against starch digestion by individual and co-existing α-amylase and amyloglucosidase</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•Epigallocatechin gallate(EGCG) inhibits amylase(AA) at slowly-digestible-starch phase.•EGCG inhibited amyloglucosidase(AMG) and AA/AMG in the whole digestion process.•Binding of EGCG with AA and AMG causes more unbound AMG in AA/AMG system.•Although EGCG-AA binding affinity was higher than EGCG-AMG, AA inhibition was weaker.•High catalytic affinity of AA to starch weakens EGCG-AA binding in digestion system.
The inhibition of (-)-epigallocatechin-gallate (EGCG) against starch digestion by α-amylase (AA), amyloglucosidase (AMG) and co-existing enzymes (AA/AMG) were comparatively studied. EGCG inhibited AA only at slowly-digestible-starch (SDS) phase. This resulted from high catalytic efficiency of AA for rapidly-digestible-starch (RDS), counteracting the inhibition at this phase. EGCG inhibited AMG and AA/AMG during whole process. At RDS phase, the catalytic velocity of AMG was always higher than AA/AMG because of an antagonistic effect of two enzymes. However, at SDS phase with EGCG, the catalytic velocity of AA/AMG was higher than AMG. This is because binding of EGCG with both enzymes caused more unbound AMG that generated more glucose in co-existing AA/AMG than AMG. Although EGCG-AA binding affinity was higher than EGCG-AMG, competitive inhibition of EGCG against AA was weaker than AMG, indicating relatively higher binding/catalyzing affinity of AA to starch significantly weakened EGCG-AA binding due to competitive relationship between starch and EGCG.</description><subject>alpha-Amylases - metabolism</subject><subject>Amylases</subject><subject>Amyloglucosidase</subject><subject>Binding interactions</subject><subject>Co-existing enzymes</subject><subject>Digestion</subject><subject>EGCG</subject><subject>Glucan 1,4-alpha-Glucosidase - metabolism</subject><subject>Starch - metabolism</subject><subject>α-Amylase</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2O0zAUhSMEYsrAK4y8ZJPinyR2WYGqUkYaiQ2sLf_ctLdK4sF2KjpvxXMg8UwkZIYtK9v3nnPPtb6iuGF0zShr3p3WbQjeHaFfc8r5mglBK_msWDElRSmp5M-LFRVUlYpVzVXxKqUTpZRTpl4WV6KulOAbuip-7YaHS4-OOJNNd3nA4UBM2-KA-UJyIGm0KUeTYa6Cy4ngcESLOcQSZisQi4OfbThkiMZlDEN6T24X2fQgFo7mjCEmElqy22_3xBwMDimTlE10R-LxAGmRXsg87Yx-NB0xgyculPADp-6U8PtnafpLZxL8bc33cOhGFxL6qfi6eNGaLsGbx_O6-PZp93X7ubz7sr_dfrwrHVcil42vhGTcMmOhBttCJeXGeMFax4Vj1lZOKee9tKoxXHnZqloZU3HFpDKtFNfF22XufQzfx2lz3WNy0HVmgDAmzZtacb5p6nqSNovUxZBShFbfR-xNvGhG9QxSn_QTSD2D1AvIyXjzmDHaHvw_2xO5SfBhEcD00zNC1MkhDA48xomT9gH_l_EH93m6GA</recordid><startdate>20220915</startdate><enddate>20220915</enddate><creator>Zhu, Shengnan</creator><creator>Li, Jing</creator><creator>Li, Wenyue</creator><creator>Li, Shuangshuang</creator><creator>Yang, Xi</creator><creator>Liu, Xuebo</creator><creator>Sun, Lijun</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20220915</creationdate><title>Enzymic catalyzing affinity to substrate affects inhibitor-enzyme binding interactions: Inhibition behaviors of EGCG against starch digestion by individual and co-existing α-amylase and amyloglucosidase</title><author>Zhu, Shengnan ; Li, Jing ; Li, Wenyue ; Li, Shuangshuang ; Yang, Xi ; Liu, Xuebo ; Sun, Lijun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c283t-6d43712b1abe5ebfe4779ad31fc23c1bb4c88cdd7b86a28d7f858aa428178af73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>alpha-Amylases - metabolism</topic><topic>Amylases</topic><topic>Amyloglucosidase</topic><topic>Binding interactions</topic><topic>Co-existing enzymes</topic><topic>Digestion</topic><topic>EGCG</topic><topic>Glucan 1,4-alpha-Glucosidase - metabolism</topic><topic>Starch - metabolism</topic><topic>α-Amylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhu, Shengnan</creatorcontrib><creatorcontrib>Li, Jing</creatorcontrib><creatorcontrib>Li, Wenyue</creatorcontrib><creatorcontrib>Li, Shuangshuang</creatorcontrib><creatorcontrib>Yang, Xi</creatorcontrib><creatorcontrib>Liu, Xuebo</creatorcontrib><creatorcontrib>Sun, Lijun</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Shengnan</au><au>Li, Jing</au><au>Li, Wenyue</au><au>Li, Shuangshuang</au><au>Yang, Xi</au><au>Liu, Xuebo</au><au>Sun, Lijun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymic catalyzing affinity to substrate affects inhibitor-enzyme binding interactions: Inhibition behaviors of EGCG against starch digestion by individual and co-existing α-amylase and amyloglucosidase</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2022-09-15</date><risdate>2022</risdate><volume>388</volume><spage>133047</spage><epage>133047</epage><pages>133047-133047</pages><artnum>133047</artnum><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•Epigallocatechin gallate(EGCG) inhibits amylase(AA) at slowly-digestible-starch phase.•EGCG inhibited amyloglucosidase(AMG) and AA/AMG in the whole digestion process.•Binding of EGCG with AA and AMG causes more unbound AMG in AA/AMG system.•Although EGCG-AA binding affinity was higher than EGCG-AMG, AA inhibition was weaker.•High catalytic affinity of AA to starch weakens EGCG-AA binding in digestion system.
The inhibition of (-)-epigallocatechin-gallate (EGCG) against starch digestion by α-amylase (AA), amyloglucosidase (AMG) and co-existing enzymes (AA/AMG) were comparatively studied. EGCG inhibited AA only at slowly-digestible-starch (SDS) phase. This resulted from high catalytic efficiency of AA for rapidly-digestible-starch (RDS), counteracting the inhibition at this phase. EGCG inhibited AMG and AA/AMG during whole process. At RDS phase, the catalytic velocity of AMG was always higher than AA/AMG because of an antagonistic effect of two enzymes. However, at SDS phase with EGCG, the catalytic velocity of AA/AMG was higher than AMG. This is because binding of EGCG with both enzymes caused more unbound AMG that generated more glucose in co-existing AA/AMG than AMG. Although EGCG-AA binding affinity was higher than EGCG-AMG, competitive inhibition of EGCG against AA was weaker than AMG, indicating relatively higher binding/catalyzing affinity of AA to starch significantly weakened EGCG-AA binding due to competitive relationship between starch and EGCG.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>35483290</pmid><doi>10.1016/j.foodchem.2022.133047</doi><tpages>1</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0308-8146 |
| ispartof | Food chemistry, 2022-09, Vol.388, p.133047-133047, Article 133047 |
| issn | 0308-8146 1873-7072 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2658229655 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | alpha-Amylases - metabolism Amylases Amyloglucosidase Binding interactions Co-existing enzymes Digestion EGCG Glucan 1,4-alpha-Glucosidase - metabolism Starch - metabolism α-Amylase |
| title | Enzymic catalyzing affinity to substrate affects inhibitor-enzyme binding interactions: Inhibition behaviors of EGCG against starch digestion by individual and co-existing α-amylase and amyloglucosidase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T21%3A38%3A43IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Enzymic%20catalyzing%20affinity%20to%20substrate%20affects%20inhibitor-enzyme%20binding%20interactions:%20Inhibition%20behaviors%20of%20EGCG%20against%20starch%20digestion%20by%20individual%20and%20co-existing%20%CE%B1-amylase%20and%20amyloglucosidase&rft.jtitle=Food%20chemistry&rft.au=Zhu,%20Shengnan&rft.date=2022-09-15&rft.volume=388&rft.spage=133047&rft.epage=133047&rft.pages=133047-133047&rft.artnum=133047&rft.issn=0308-8146&rft.eissn=1873-7072&rft_id=info:doi/10.1016/j.foodchem.2022.133047&rft_dat=%3Cproquest_cross%3E2658229655%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2658229655&rft_id=info:pmid/35483290&rft_els_id=S0308814622010093&rfr_iscdi=true |