In Vitro Inhibition of Pancreatic Lipase by Polyphenols: A Kinetic, Fluorescence Spectroscopy and Molecular Docking Study
The inhibitory activity and binding characteristics of caffeic acid, -coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC =(6.1±2.4)...
Saved in:
| Published in | Food technology and biotechnology Vol. 55; no. 4; pp. 519 - 530 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Croatia
Sveuciliste U Zagrebu
01.10.2017
Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet University of Zagreb Faculty of Food Technology and Biotechnology |
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | The inhibitory activity and binding characteristics of caffeic acid,
-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC
=(6.1±2.4) µM), followed by
-coumaric acid ((170.2±20.6) µM) and caffeic acid ((401.5±32.1) µM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and
-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and
-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. |
|---|---|
| AbstractList | The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC50=(6.1±2.4) µM), followed by p-coumaric acid ((170.2±20.6) µM) and caffeic acid ((401.5±32.1) µM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. The inhibitory activity and binding characteristics of caffeic acid, p -coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC 50 =(6.1±2.4) µM), followed by p -coumaric acid ((170.2±20.6) µM) and caffeic acid ((401.5±32.1) µM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p -coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p -coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC50=(6.1±2.4) µM), followed by p-coumaric acid ((170.2±20.6) µM) and caffeic acid ((401.5±32.1) µM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed.The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC50=(6.1±2.4) µM), followed by p-coumaric acid ((170.2±20.6) µM) and caffeic acid ((401.5±32.1) µM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor ([IC.sub.50] =(6.1[+ or -]2.4) [micro]M), followed by p-coumaric acid ((170.2[+ or -]20.6) [micro]M) and caffeic acid ((401.5[+ or -]32.1) [micro]M), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and n-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. Key words: polyphenolic compounds, pancreatic lipase, enzymatic inhibition, molecular docking, anti-obesity effect The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor ([IC.sub.50] =(6.1[+ or -]2.4) [micro]M), followed by p-coumaric acid ((170.2[+ or -]20.6) [micro]M) and caffeic acid ((401.5[+ or -]32.1) [micro]M), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and n-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. The inhibitory activity and binding characteristics of caffeic acid, -coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC =(6.1±2.4) µM), followed by -coumaric acid ((170.2±20.6) µM) and caffeic acid ((401.5±32.1) µM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and -coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and -coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC50=(6.1±2.4) μM), followed by p-coumaric acid ((170.2±20.6) μM) and caffeic acid ((401.5±32.1) μM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. |
| Audience | Academic |
| Author | Alvarez-Parrilla, Emilio Díaz-Sánchez, Ángel G. Martinez-Gonzalez, Alejandra I. Vazquez-Flores, Alma A. Núñez-Gastélum, José A. Gonzalez-Aguilar, Gustavo A. de la Rosa, Laura A. |
| Author_xml | – sequence: 1 givenname: Alejandra I. orcidid: 0000-0002-0248-9175 surname: Martinez-Gonzalez fullname: Martinez-Gonzalez, Alejandra I. – sequence: 2 givenname: Emilio orcidid: 0000-0002-6162-8139 surname: Alvarez-Parrilla fullname: Alvarez-Parrilla, Emilio – sequence: 3 givenname: Ángel G. orcidid: 0000-0002-6398-7274 surname: Díaz-Sánchez fullname: Díaz-Sánchez, Ángel G. – sequence: 4 givenname: Laura A. orcidid: 0000-0003-2082-873X surname: de la Rosa fullname: de la Rosa, Laura A. – sequence: 5 givenname: José A. orcidid: 0000-0002-7098-4485 surname: Núñez-Gastélum fullname: Núñez-Gastélum, José A. – sequence: 6 givenname: Alma A. orcidid: 0000-0003-2685-0049 surname: Vazquez-Flores fullname: Vazquez-Flores, Alma A. – sequence: 7 givenname: Gustavo A. orcidid: 0000-0002-7452-286X surname: Gonzalez-Aguilar fullname: Gonzalez-Aguilar, Gustavo A. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29540986$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9kktvEzEUhUeoiD7gD7BAltiwIGH8jM0CKSoUIoKoVGBreezrxGFiD_NAmn-Pk7SoqRDywr72uZ917HNenMQUoSie43KKZxjTN76vppxPS5brKcdUPirOMKVsQkQpTvbrcqKkIKfFeddtypLKmcJPilOiOCvzwVkxLiL6Efo2oUVchyr0IUWUPLo20bZg-mDRMjSmA1SN6DrVY7OGmOruLZqjzyFCFrxGV_WQWugsRAvopgGbeZ1NzYhMdOhLqsEOtWnR-2R_hrhCN_3gxqfFY2_qDp7dzhfF96sP3y4_TZZfPy4u58uJ5YL2EwfWuVJ4M3OV95TQCioqBJ0B46WRwAl2yhNwzkvA0ivhmWCCgGUOK1PRi2Jx4LpkNrppw9a0o04m6P1GalfatNlGDVpKTB11EnMAVlmrpFQeK-lxNWMVgcx6d2A1Q7UFlw33ramPoMcnMaz1Kv3WXDKJlciAV7eANv0aoOv1NuR3q2sTIQ2dJiVmmGWXKktfPpBu0tDG_FQaK6UY5_y-amWygRB9yvfaHVTPORFyhgljWTX9hyoPB9tgc6p8yPtHDS_uG_3r8C44WSAPApu_umvBaxt6s0tPJoda41LvM6pzRjXnumS51ruM5lbyoPWO_p-mP8ga6wM |
| CitedBy_id | crossref_primary_10_1590_0103_8478cr20200778 crossref_primary_10_1016_j_jff_2024_106258 crossref_primary_10_1007_s12291_023_01165_w crossref_primary_10_1007_s11694_020_00654_3 crossref_primary_10_1016_j_hermed_2021_100508 crossref_primary_10_1080_10408398_2023_2217264 crossref_primary_10_1039_D1FO00382H crossref_primary_10_1016_j_foodhyd_2025_111310 crossref_primary_10_1016_j_arabjc_2023_105486 crossref_primary_10_1055_a_1891_3588 crossref_primary_10_7717_peerj_7022 crossref_primary_10_1039_D2RA06715C crossref_primary_10_1155_2020_6769726 crossref_primary_10_1016_j_lwt_2020_110032 crossref_primary_10_1016_j_indcrop_2019_111778 crossref_primary_10_1016_j_jff_2021_104479 crossref_primary_10_3389_fnut_2021_772903 crossref_primary_10_1016_j_lwt_2024_115854 crossref_primary_10_61975_gjset_v2i1_23 crossref_primary_10_1016_j_algal_2023_103331 crossref_primary_10_1016_j_saa_2022_122240 crossref_primary_10_1155_2024_6638781 crossref_primary_10_1007_s42250_023_00790_5 crossref_primary_10_4155_fmc_2019_0284 crossref_primary_10_1016_j_jff_2023_105458 crossref_primary_10_1016_j_lwt_2021_112674 crossref_primary_10_1016_j_bmcl_2023_129574 crossref_primary_10_1080_19476337_2023_2294994 crossref_primary_10_1080_09168451_2018_1498726 crossref_primary_10_1080_14756366_2023_2269481 crossref_primary_10_1016_j_foodres_2024_114776 crossref_primary_10_1111_ijfs_17115 crossref_primary_10_1016_j_fochms_2021_100020 crossref_primary_10_1016_j_ijbiomac_2024_134092 crossref_primary_10_1111_ijfs_16428 crossref_primary_10_1016_j_jfca_2021_104293 crossref_primary_10_1016_j_lwt_2023_114643 crossref_primary_10_1016_j_jff_2020_104041 crossref_primary_10_1016_j_ijbiomac_2020_10_219 crossref_primary_10_1111_jfbc_13282 crossref_primary_10_1016_j_talanta_2020_121948 crossref_primary_10_1038_s41598_024_80197_5 crossref_primary_10_1016_j_jff_2023_105913 crossref_primary_10_1016_j_fbio_2024_105438 crossref_primary_10_1016_j_jep_2022_115670 crossref_primary_10_1039_D3RA05826C crossref_primary_10_1016_j_fbio_2023_103414 crossref_primary_10_1016_j_fbio_2022_101992 crossref_primary_10_1007_s11030_024_11005_5 crossref_primary_10_1111_cbdd_14443 crossref_primary_10_2139_ssrn_4136031 crossref_primary_10_1016_j_fbio_2020_100658 crossref_primary_10_1016_j_biopha_2020_110143 crossref_primary_10_1080_10408398_2023_2299329 crossref_primary_10_1016_j_foodchem_2020_127528 crossref_primary_10_1016_j_foodchem_2022_134192 crossref_primary_10_1016_j_jbiotec_2024_02_011 crossref_primary_10_1016_j_jff_2022_105125 crossref_primary_10_1016_j_jff_2021_104710 crossref_primary_10_3407_rpn_v5i2_6823 crossref_primary_10_1021_acsfoodscitech_1c00415 crossref_primary_10_1021_acsomega_3c07227 crossref_primary_10_1021_acs_jnatprod_0c01387 crossref_primary_10_1016_j_ijbiomac_2021_10_010 crossref_primary_10_1155_2024_2350186 crossref_primary_10_1155_2022_4145659 crossref_primary_10_1016_j_bpc_2020_106409 crossref_primary_10_1080_14756366_2022_2029855 crossref_primary_10_1016_j_algal_2020_101980 crossref_primary_10_1016_j_molliq_2021_116505 crossref_primary_10_2174_1570180819666220314094820 crossref_primary_10_1039_D2FO03219H crossref_primary_10_1016_j_molstruc_2025_141748 crossref_primary_10_1007_s13205_022_03309_w crossref_primary_10_1007_s10811_022_02900_1 crossref_primary_10_1016_j_ijbiomac_2020_05_215 crossref_primary_10_1016_j_ijbiomac_2020_07_305 crossref_primary_10_1016_j_foodchem_2022_132106 crossref_primary_10_1016_j_dyepig_2022_110545 crossref_primary_10_1016_j_biochi_2020_08_016 crossref_primary_10_1016_j_jff_2021_104892 crossref_primary_10_1080_10408398_2025_2474177 crossref_primary_10_1016_j_foodchem_2021_129960 crossref_primary_10_1080_10408398_2021_1927977 crossref_primary_10_1111_1750_3841_14386 crossref_primary_10_1080_10408347_2020_1797467 crossref_primary_10_21448_ijsm_1084743 crossref_primary_10_1016_j_fct_2018_08_071 crossref_primary_10_1016_j_jep_2020_112961 crossref_primary_10_3407_rpn_v5i2_6859 crossref_primary_10_1111_jfbc_14325 crossref_primary_10_1016_j_foodres_2022_111552 crossref_primary_10_1016_j_phytol_2022_06_011 crossref_primary_10_1016_j_saa_2018_08_057 crossref_primary_10_1080_10408347_2023_2221731 crossref_primary_10_1371_journal_pone_0224853 crossref_primary_10_3389_fnut_2023_1177897 |
| ContentType | Journal Article |
| Copyright | COPYRIGHT 2017 Sveuciliste U Zagrebu Copyright Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet 2017 2017 University of Zagreb Faculty of Food Technology and Biotechnology |
| Copyright_xml | – notice: COPYRIGHT 2017 Sveuciliste U Zagrebu – notice: Copyright Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet 2017 – notice: 2017 University of Zagreb Faculty of Food Technology and Biotechnology |
| CorporateAuthor | Research Center for Food & Development, A.C. (CIAD), Carretera a Ejido La Victoria, Km. 0.6, Hermosillo, Sonora 83304, Mexico Department of Chemical Biological Sciences, Institute for Biomedical Sciences, Autonomous University of Juarez City, 1210 Plutarco Elias Calles Ave., Juarez, Chihuahua, Mexico |
| CorporateAuthor_xml | – name: Research Center for Food & Development, A.C. (CIAD), Carretera a Ejido La Victoria, Km. 0.6, Hermosillo, Sonora 83304, Mexico – name: Department of Chemical Biological Sciences, Institute for Biomedical Sciences, Autonomous University of Juarez City, 1210 Plutarco Elias Calles Ave., Juarez, Chihuahua, Mexico |
| DBID | AAYXX CITATION NPM 3V. 7QO 7RQ 7T7 7X2 7XB 8FD 8FE 8FG 8FH 8FK 8G5 ABJCF ABUWG AEUYN AFKRA ATCPS AZQEC BBNVY BENPR BGLVJ BHPHI BYOGL C1K CCPQU DWQXO FR3 GNUQQ GUQSH HCIFZ L6V LK8 M0K M2O M7P M7S MBDVC P64 PHGZM PHGZT PIMPY PKEHL PQEST PQGLB PQQKQ PQUKI PRINS PTHSS Q9U 7X8 5PM DOA |
| DOI | 10.17113/ftb.55.04.17.5138 |
| DatabaseName | CrossRef PubMed ProQuest Central (Corporate) Biotechnology Research Abstracts Career & Technical Education Database Industrial and Applied Microbiology Abstracts (Microbiology A) Agricultural Science Collection ProQuest Central (purchase pre-March 2016) Technology Research Database ProQuest SciTech Collection ProQuest Technology Collection ProQuest Natural Science Journals ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Research Library Materials Science & Engineering Collection ProQuest Central (Alumni) ProQuest One Sustainability ProQuest Central UK/Ireland Agricultural & Environmental Science Collection ProQuest Central Essentials Biological Science Collection ProQuest Central Technology Collection Natural Science Collection ProQuest East Europe, Central Europe Database (NC LIVE) Environmental Sciences and Pollution Management ProQuest One ProQuest Central Engineering Research Database ProQuest Central Student ProQuest Research Library SciTech Premium Collection ProQuest Engineering Collection Biological Sciences Agricultural Science Database Research Library (ProQuest) Biological Science Database Engineering Database Research Library (Corporate) Biotechnology and BioEngineering Abstracts ProQuest Central Premium ProQuest One Academic Publicly Available Content Database (ProQuest) ProQuest One Academic Middle East (New) ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China Engineering Collection ProQuest Central Basic MEDLINE - Academic PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals |
| DatabaseTitle | CrossRef PubMed Agricultural Science Database Publicly Available Content Database Research Library Prep ProQuest Central Student Technology Collection Technology Research Database ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College Research Library (Alumni Edition) ProQuest Natural Science Collection ProQuest Central China Environmental Sciences and Pollution Management ProQuest Central ProQuest One Applied & Life Sciences ProQuest One Sustainability ProQuest Engineering Collection Biotechnology Research Abstracts Natural Science Collection ProQuest Central Korea Agricultural & Environmental Science Collection Biological Science Collection ProQuest Research Library Industrial and Applied Microbiology Abstracts (Microbiology A) ProQuest Central (New) Engineering Collection Engineering Database ProQuest Biological Science Collection ProQuest Central Basic ProQuest One Academic Eastern Edition East Europe, Central Europe Database Agricultural Science Collection ProQuest Technology Collection Biological Science Database ProQuest SciTech Collection Biotechnology and BioEngineering Abstracts ProQuest Career and Technical Education ProQuest One Academic UKI Edition Materials Science & Engineering Collection Engineering Research Database ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic |
| DatabaseTitleList | Agricultural Science Database MEDLINE - Academic PubMed |
| Database_xml | – sequence: 1 dbid: DOA name: DOAJ (Directory of Open Access Journals) url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: 8FG name: ProQuest Technology Collection url: https://search.proquest.com/technologycollection1 sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Engineering |
| EISSN | 1334-2606 |
| EndPage | 530 |
| ExternalDocumentID | oai_doaj_org_article_8813d3d815ee4bcc9889f198f1b74b2e PMC5848196 A526871244 29540986 10_17113_ftb_55_04_17_5138 |
| Genre | Journal Article |
| GeographicLocations | Mexico New York United States--US |
| GeographicLocations_xml | – name: Mexico – name: New York – name: United States--US |
| GroupedDBID | 29H 2WC 4P2 5GY 5VS 7RQ 7X2 8FE 8FG 8FH 8G5 8VB A8Z AAFWJ AAKDD AAYXX ABJCF ABUWG ACGFO ACIWK ACPRK ADBBV ADDVE AENEX AEUYN AFKRA AFRAH AHQJS AKVCP ALMA_UNASSIGNED_HOLDINGS AOIJS APEBS ATCPS AZQEC BBNVY BCNDV BENPR BGLVJ BHPHI BPHCQ BYOGL C1A CCPQU CITATION DWQXO DYU E3Z EBD EBS EBU ECGQY EDH EJD EN8 EOJEC ESTFP GNUQQ GROUPED_DOAJ GUQSH GX1 HCIFZ HYE I-F IAG IAO ICU IPNFZ ITC ITG ITH K1G KQ8 L6V LK8 M0K M2O M7P M7S ML0 OBODZ OK1 OVT OZF PHGZM PHGZT PIMPY PQQKQ PROAC PTHSS PV9 QWB RIG RNS RPM RZL TH9 TR2 VP8 XSB ZL0 ~8M NPM PQGLB PMFND 3V. 7QO 7T7 7XB 8FD 8FK C1K FR3 MBDVC P64 PKEHL PQEST PQUKI PRINS Q9U 7X8 5PM PUEGO |
| ID | FETCH-LOGICAL-c563t-decdd06fa7dbff323beb36637e450a8e521d9f2eddf8e18f96f46462ec4d19ab3 |
| IEDL.DBID | DOA |
| ISSN | 1330-9862 |
| IngestDate | Wed Aug 27 01:26:56 EDT 2025 Thu Aug 21 18:03:25 EDT 2025 Fri Jul 11 02:48:31 EDT 2025 Fri Jul 25 08:56:54 EDT 2025 Tue Jun 17 21:33:46 EDT 2025 Tue Jun 10 20:35:03 EDT 2025 Mon Jul 21 06:02:14 EDT 2025 Tue Jul 01 03:54:09 EDT 2025 Thu Apr 24 23:12:46 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 4 |
| Keywords | anti-obesity effect enzymatic inhibition molecular docking polyphenolic compounds pancreatic lipase |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c563t-decdd06fa7dbff323beb36637e450a8e521d9f2eddf8e18f96f46462ec4d19ab3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| ORCID | 0000-0002-6162-8139 0000-0002-7098-4485 0000-0002-6398-7274 0000-0002-7452-286X 0000-0002-0248-9175 0000-0003-2685-0049 0000-0003-2082-873X |
| OpenAccessLink | https://doaj.org/article/8813d3d815ee4bcc9889f198f1b74b2e |
| PMID | 29540986 |
| PQID | 1999455539 |
| PQPubID | 946363 |
| PageCount | 12 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_8813d3d815ee4bcc9889f198f1b74b2e pubmedcentral_primary_oai_pubmedcentral_nih_gov_5848196 proquest_miscellaneous_2014143239 proquest_journals_1999455539 gale_infotracmisc_A526871244 gale_infotracacademiconefile_A526871244 pubmed_primary_29540986 crossref_citationtrail_10_17113_ftb_55_04_17_5138 crossref_primary_10_17113_ftb_55_04_17_5138 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2017-10-01 |
| PublicationDateYYYYMMDD | 2017-10-01 |
| PublicationDate_xml | – month: 10 year: 2017 text: 2017-10-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Croatia |
| PublicationPlace_xml | – name: Croatia – name: Zagreb |
| PublicationTitle | Food technology and biotechnology |
| PublicationTitleAlternate | Food Technol Biotechnol |
| PublicationYear | 2017 |
| Publisher | Sveuciliste U Zagrebu Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet University of Zagreb Faculty of Food Technology and Biotechnology |
| Publisher_xml | – name: Sveuciliste U Zagrebu – name: Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet – name: University of Zagreb Faculty of Food Technology and Biotechnology |
| SSID | ssj0038791 |
| Score | 2.4999325 |
| Snippet | The inhibitory activity and binding characteristics of caffeic acid,
-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper,... The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper,... The inhibitory activity and binding characteristics of caffeic acid, p -coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper,... |
| SourceID | doaj pubmedcentral proquest gale pubmed crossref |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source |
| StartPage | 519 |
| SubjectTerms | Amino acids anti-obesity effect Binding sites Caffeic acid Cancer Capsaicin Capsicum annuum Care and treatment enzymatic inhibition Enzymes Fluorescence Fluorescence spectroscopy Hydrogen bonding Hydrogen bonds Hydrophobicity Ligands Lipase Molecular biology Molecular docking Obesity Original Scientific Papers p-Coumaric acid Pancreas pancreatic lipase Phenolic compounds Phenols polyphenolic compounds Polyphenols Quercetin Risk factors Spectroscopic analysis Spectroscopy Spectrum analysis |
| SummonAdditionalLinks | – databaseName: ProQuest Central dbid: BENPR link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3db9MwELdge4EHxDfZBjISEg-Qrf6MzQvq0KoN2FQhJu3Nir9YpSopbYrU_x5fmpZGSHtMfI5i3_k-7PPvEHrnQxy4wMtcU89zLm2Rl8zKXLpETr0oaQvqc3klz6_51xtx0224Lbq0yo1ObBW1rx3skZ_AdXkuhGD68-x3DlWj4HS1K6FxH-0nFaxS8LV_enY1_rHRxUwVeh1ysUGuk_PeXZspCGEnsbHHQgDQKSmOBYEbKjumqUXw_19P7xiqfhLljlUaPUaPOncSD9f8f4LuheopergDMvgMrS4q_GfSzGt8Ud1ObJuiheuIx4nfrcfo8PfJLBkzbFd4XE9XkPVVTxef8BB_S59JBB_xaLqs5y3ykwsYatY3gIJZz1a4rDy-3NTYxclmwd47hvTE1XN0PTr7-eU87wou5E5I1uQ-OO8HMpaFtzEyymwKtZNLUgQuBqUKydR7HWnwPqpAVNQycsklDY57okvLXqC9qq7CK4Qpt4Az45M_ongZSyukjYp6x6N2UfIMkc1cG9ehkUNRjKmBqAT4YxJ_jBBmwNOzAf5k6MO2z2yNxXEn9SmwcEsJONrti3r-y3TL0ihFmGdeERECt85ppXQkWkViC25pyNB7EAADqz39niu7SwtpkICbZYaAllOAj5Shox5lWqWu37wRIdNpiYX5J9MZertthp6Q-VaFerkwFDJxeeJFonm5lrjtkOCMNs2vzFDRk8XemPst1eS2xRAXUEZBy4O7f-sQPaDgxrTJi0dor5kvw-vkhDX2TbfS_gKwtDKx priority: 102 providerName: ProQuest |
| Title | In Vitro Inhibition of Pancreatic Lipase by Polyphenols: A Kinetic, Fluorescence Spectroscopy and Molecular Docking Study |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/29540986 https://www.proquest.com/docview/1999455539 https://www.proquest.com/docview/2014143239 https://pubmed.ncbi.nlm.nih.gov/PMC5848196 https://doaj.org/article/8813d3d815ee4bcc9889f198f1b74b2e |
| Volume | 55 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3da9swEBdb97I9jH3Xaxc0GOxhcxtbH5b3lo5m7baWMBbonoT1RQPBDolTyH-_O9sJMYPtZS8GWycj3Z10d_bpd4S8cz4MredFnKeOx1yaLC6YkbG0QJ46UaQNqM_VtbyY8q834mav1BfmhLXwwC3jTpVKmGNOJcJ7bqzNlcoDRMohMRk3qcfdF2zeNphq92CmsrwNtdgwzsFp747LZEnCTkNtToRAgNMkOxEJnkzZM0kNcv-f-_OegeonT-5Zo_ET8rhzI-moHf5Tcs-Xz8ijPXDB52RzWdK7Wb2s6GV5OzNNahatAp2AnBtP0dLvswUYMWo2dFLNN5jtVc1Xn-iIfoPXAMFHOp6vq2WD-GQ9xVr1NaJfVosNLUpHr7a1dSnYKvzmTjEtcfOCTMfnPz9fxF2hhdgKyerYeevcUIYicyYEljIDITa4IpnnYlgoDybe5SH1zgXlExVyGbjkMvWWuyQvDHtJDsqq9IeEptwgvowDP0TxIhRGSBNU6iwPuQ2SRyTZ8lrbDoUci2HMNUYjKB8N8tFC6CGHe43yiciHXZ9Fi8HxV-ozFOGOEvGzmwegVbrTKv0vrYrIe1QAjaschmeL7rACTBLxsvQIUXIy9I0ictyjhNVp-81bFdLd7rDSCP3AhRAsj8jbXTP2xIy30lfrlU4xA5eDLIDmVatxuynhv1ngr4xI1tPF3pz7LeXstsEOF1g-IZev_weTjsjDFJ2cJrXxmBzUy7V_Ay5abQbkvhp_GZAHZ-fXkx-DZm3i9df0N1TOPYU |
| linkProvider | Directory of Open Access Journals |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwzV1Lb9NAEF6V9gAceD8CBRYJxAGcxuvdtY3EoQVKQ5JSiVYqp8X7ohGRXeUBMn-Fv8KPY8axQwJSb5U4Ojt-7Hp2HvE33xDyxDrfMY5nQcosD7jUcZBFWgbSgDizImMVqc9gX-4d8ffH4niN_GxqYRBW2djEylDbwuB_5FtYLs-FEFFaIyh7rvwO-dnkVfcNvMynjO2-PXy9F9QtBAIjZDQNrDPWdqTPYqu9j1ikIXkEJxs7LjpZ4sB52dQzZ61PXJj4VHouuWTOcBummY7guhfIBmQVTKyTjZ1PH971G0MfJXE6z-eiTpBCZlDX5MRhGG35qW4LgSyqYdwWIZa_LPm9qj3Av05gyQuuIjSXXN7uVfKrWaw50uVrewY3Mz_-4pH8T1fzGrlSh9p0e743rpM1l98gl5cIGG-SspvTb8PpuKDd_GSoK_gaLTw9gL1QRdOG9oen4OipLulBMSoREVeMJi_pNu3BZUDgBd0dzYpxxYplHP14WrUVwmKfkma5pYOm_zAFf47fJShCN8tb5Ohc5n6brOdF7u4SyrhGDh4LsVrCM59pIbVPmDXcp8ZL3iJhoyrK1Ezt2DBkpDBjQ_VSoF5KCNXhcKxQvVrk-eKc0zlPyZnSO6iBC0nkGK9-KMZfVG2yVJKEkY1sEgrnuDYmTZLUh2niQx1zzVyLPEP9VWgJ4fFMVhd0wCSRU0xtI5NQjPFji2yuSIIFM6vDjZKq2oJO1B8NbZHHi2E8E1GBuStmE8UQpczhXYDMnfmGWUwJv1_D-soWiVe20sqcV0fy4UnFry6wxUQq7539WI_Ixb3DQV_1u_u9--QSw3CvAnlukvXpeOYeQLA61Q9ro0HJ5_PeWb8Bx2unYQ |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV3db9MwELdGJyF4QHxTGGAkEA-QtXFsJ0FCqGOrVrpVFWzS3kz8xSpVSekHqP8afx13aVJaIe1tj4nPUew730dy9ztCXlvn28bxLEiZ5QGXOg6ySMtAGiBnVmSsBPU5Hcjjc_7lQlzskD91LQymVdY6sVTUtjD4jbyF5fJcCBGlLV-lRQwPu58mPwPsIIV_Wut2GisR6bvlbwjfZh97h8DrN4x1j84-HwdVh4HACBnNA-uMtW3ps9hq7yMWaYgtwQbHjot2ljiwbTb1zFnrExcmPpWeSy6ZM9yGaaYjeO4NshtDVNRukN2Do8Hwa20HoiROV-Fe1A5SCByqkp04DKOWn-t9IRBkNYz3RYjVMRtmsewe8L-N2DCS2wmcGxaxe5fcqVxZ2lnJ3j2y4_L75PYGwOEDsuzl9NdoPi1oL78c6TI9jBaeDkHWSm_V0JPRBAwp1Us6LMZLzDgrxrMPtEP78BggeE-740UxLVGnjKPfJmXbHiymWdIst_S07u9LwV7id3-KqZHLh-T8WljxiDTyIndPCGVcI8aNBV8o4ZnPtJDaJ8wa7lPjJW-SsN5rZSokdGzIMVYYESF_FPBHCaHaHK4V8qdJ3q3nTFY4IFdSHyAL15SI4V3eKKY_VKUSVJKEkY1sEgrnuDYmTZLUh2niQx1zzVyTvEUBUKhp4PVMVhVMwCIRs0t1EKknRv-sSfa2KEFDmO3hWoRUpaFm6t95apJX62GciVl3uSsWM8UwC5gDL4Dm8Uri1kvC_8Owv7JJ4i1Z3Frz9kg-uizxywW2cEjl06tf6yW5CQdcnfQG_WfkFkNvqsyh3CON-XThnoMvONcvqkNHyffrPud_Afbfdks |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=In+vitro+Inhibition+of+Pancreatic+Lipase+by+Polyphenols%3A%E2%80%A8A+Kinetic%2C+Fluorescence+Spectroscopy+and+Molecular+Docking+Study&rft.jtitle=Food+technology+and+biotechnology&rft.au=Martinez-Gonzalez%2C+Alejandra+I&rft.au=Alvarez-Parrilla%2C+Emilio&rft.au=D%C3%ADaz-S%C3%A1nchez%2C+%C3%81ngel+G&rft.au=de+la+Rosa%2C+Laura+A&rft.date=2017-10-01&rft.issn=1330-9862&rft.volume=55&rft.issue=4&rft.spage=519&rft_id=info:doi/10.17113%2Fftb.55.04.17.5138&rft_id=info%3Apmid%2F29540986&rft.externalDocID=29540986 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1330-9862&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1330-9862&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1330-9862&client=summon |