133 related articles for article (PubMed ID: 36596106)
1. Inconsistency between polyphenol-enzyme binding interactions and enzyme inhibition: Galloyl moiety decreases amyloglucosidase inhibition of catechins.
Zhang J; Li S; Liu X; Sun L
Food Res Int; 2023 Jan; 163():112155. PubMed ID: 36596106
[TBL] [Abstract][Full Text] [Related]
2. 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.
Zhu S; Li J; Li W; Li S; Yang X; Liu X; Sun L
Food Chem; 2022 Sep; 388():133047. PubMed ID: 35483290
[TBL] [Abstract][Full Text] [Related]
3. The galloyl moiety enhances the inhibitory activity of catechins and theaflavins against α-glucosidase by increasing the polyphenol-enzyme binding interactions.
Sun L; Song Y; Chen Y; Ma Y; Fu M; Liu X
Food Funct; 2021 Jan; 12(1):215-229. PubMed ID: 33295908
[TBL] [Abstract][Full Text] [Related]
4. α-Amylase Changed the Catalytic Behaviors of Amyloglucosidase Regarding Starch Digestion Both in the Absence and Presence of Tannic Acid.
Li S; Wu W; Li J; Zhu S; Yang X; Sun L
Front Nutr; 2022; 9():817039. PubMed ID: 35495955
[TBL] [Abstract][Full Text] [Related]
5. The mechanism of interactions between tea polyphenols and porcine pancreatic alpha-amylase: Analysis by inhibition kinetics, fluorescence quenching, differential scanning calorimetry and isothermal titration calorimetry.
Sun L; Gidley MJ; Warren FJ
Mol Nutr Food Res; 2017 Oct; 61(10):. PubMed ID: 28618113
[TBL] [Abstract][Full Text] [Related]
6. Revealing the mechanisms of starch amylolysis affected by tea catechins using surface plasmon resonance.
Xu H; Zhou J; Yu J; Wang S; Copeland L; Wang S
Int J Biol Macromol; 2020 Feb; 145():527-534. PubMed ID: 31870878
[TBL] [Abstract][Full Text] [Related]
7. Mutual interactions between α-amylase and amyloglucosidase in the digestion of starch with distinct chain-length distributions at a fully gelatinized state.
Zhou X; Wang C; Yue S; Zheng Y; Li C; Yu W
Food Funct; 2022 Mar; 13(6):3453-3464. PubMed ID: 35244103
[TBL] [Abstract][Full Text] [Related]
8. Number of galloyl moieties and molecular flexibility are both important in alpha-amylase inhibition by galloyl-based polyphenols.
Cao J; Zhang Y; Han L; Zhang S; Duan X; Sun L; Wang M
Food Funct; 2020 May; 11(5):3838-3850. PubMed ID: 32319456
[TBL] [Abstract][Full Text] [Related]
9. Tea polyphenols enhance binding of porcine pancreatic α-amylase with starch granules but reduce catalytic activity.
Sun L; Gidley MJ; Warren FJ
Food Chem; 2018 Aug; 258():164-173. PubMed ID: 29655719
[TBL] [Abstract][Full Text] [Related]
10. Number of galloyl moiety and intramolecular bonds in galloyl-based polyphenols affect their interaction with alpha-glucosidase.
Cao J; Yan S; Xiao Y; Han L; Sun L; Wang M
Food Chem; 2022 Jan; 367():129846. PubMed ID: 34399273
[TBL] [Abstract][Full Text] [Related]
11. Three flavanols delay starch digestion by inhibiting α-amylase and binding with starch.
Jiang C; Chen Y; Ye X; Wang L; Shao J; Jing H; Jiang C; Wang H; Ma C
Int J Biol Macromol; 2021 Mar; 172():503-514. PubMed ID: 33454330
[TBL] [Abstract][Full Text] [Related]
12. Inhibition of α-amylase and amyloglucosidase by cellulose nanofibrils with different surface charge and spectroscopic analysis of their interaction mechanism.
Zhang K; Tian X; Shen R; Wang Y; Zhang Y; Wang W
Food Res Int; 2023 Aug; 170():113053. PubMed ID: 37316033
[TBL] [Abstract][Full Text] [Related]
13. Essential moieties of myricetins, quercetins and catechins for binding and inhibitory activity against α-Glucosidase.
Fu M; Shen W; Gao W; Namujia L; Yang X; Cao J; Sun L
Bioorg Chem; 2021 Oct; 115():105235. PubMed ID: 34388484
[TBL] [Abstract][Full Text] [Related]
14. Comparison of porous starches obtained from different enzyme types and levels.
Benavent-Gil Y; Rosell CM
Carbohydr Polym; 2017 Feb; 157():533-540. PubMed ID: 27987959
[TBL] [Abstract][Full Text] [Related]
15. α-Amylase inhibition of a certain dietary polyphenol is predominantly affected by the concentration of α-1, 4-glucosidic bonds in starchy and artificial substrates.
Zhang J; Li C; Wang G; Cao J; Yang X; Liu X; Sun L
Food Res Int; 2022 Jul; 157():111210. PubMed ID: 35761532
[TBL] [Abstract][Full Text] [Related]
16. The interplay of α-amylase and amyloglucosidase activities on the digestion of starch in in vitro enzymic systems.
Warren FJ; Zhang B; Waltzer G; Gidley MJ; Dhital S
Carbohydr Polym; 2015 Mar; 117():192-200. PubMed ID: 25498625
[TBL] [Abstract][Full Text] [Related]
17. Molecular insights into α-glucosidase inhibition and antiglycation properties affected by the galloyl moiety in (-)-epigallocatechin-3-gallate.
Guan Q; Tang L; Zhang L; Huang L; Xu M; Wang Y; Zhang M
J Sci Food Agric; 2023 Dec; 103(15):7381-7392. PubMed ID: 37390299
[TBL] [Abstract][Full Text] [Related]
18. Caffeoyl substitution decreased the binding and inhibitory activity of quinic acid against α-amylase: The reason why chlorogenic acid is a relatively weak enzyme inhibitor.
Song Y; Li W; Yang H; Peng X; Yang X; Liu X; Sun L
Food Chem; 2022 Mar; 371():131278. PubMed ID: 34808763
[TBL] [Abstract][Full Text] [Related]
19. Inhibition of in vitro enzymatic starch digestion by coffee extract.
Li X; Cai J; Yu J; Wang S; Copeland L; Wang S
Food Chem; 2021 Oct; 358():129837. PubMed ID: 33940299
[TBL] [Abstract][Full Text] [Related]
20. Inhibition of α-amylase digestion by a Lonicera caerulea berry polyphenol starch complex revealed via multi-spectroscopic and molecular dynamics analyses.
Liu S; Meng F; Guo S; Yuan M; Wang H; Chang X
Int J Biol Macromol; 2024 Mar; 260(Pt 2):129573. PubMed ID: 38266829
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
