Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion. / Xu, Jinchuan; Blennow, Andreas; Liu, Xingxun; Wang, Shujun.

I: ACS Food Science & Technology, Bind 3, Nr. 9, 2023, s. 1532-1539.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Xu, J, Blennow, A, Liu, X & Wang, S 2023, 'Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion', ACS Food Science & Technology, bind 3, nr. 9, s. 1532-1539. https://doi.org/10.1021/acsfoodscitech.3c00192

APA

Xu, J., Blennow, A., Liu, X., & Wang, S. (2023). Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion. ACS Food Science & Technology, 3(9), 1532-1539. https://doi.org/10.1021/acsfoodscitech.3c00192

Vancouver

Xu J, Blennow A, Liu X, Wang S. Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion. ACS Food Science & Technology. 2023;3(9):1532-1539. https://doi.org/10.1021/acsfoodscitech.3c00192

Author

Xu, Jinchuan ; Blennow, Andreas ; Liu, Xingxun ; Wang, Shujun. / Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion. I: ACS Food Science & Technology. 2023 ; Bind 3, Nr. 9. s. 1532-1539.

Bibtex

@article{171bdcd5847246f8afcf8caef7b34d66,
title = "Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion",
abstract = "The purpose of this study was to investigate the effects of tea polyphenols (TPs) on the activity of starch digestion enzymes, including α-amylase, pancreatin, and amyloglucosidase (AMG), which simulate the digestion process in the oral cavity, stomach, and small intestine, respectively. We determined the main polyphenol composition of green tea polyphenols using high-performance liquid chromatography (HPLC), with a focus on epicatechin (EC), epigallocatechin (EGC), epigallocatechin gallate (EGCG), and epicatechin gallate (ECG). When mixed with hydrolytic enzymes, the fluorescence emission spectra data revealed a significant decrease in the fluorescence intensity of TPs over time, indicating an increased interaction between TPs and the hydrolytic enzymes with increasing TPs concentration within the measured range. The inhibition percentage (%) and fluorescence emission spectral data demonstrated an initial increase in the inhibition of TPs with increasing concentration, followed by a plateau. Moreover, molecular docking studies revealed that EGC exhibited a higher affinity than did the other catechins, resulting in the formation of more hydrogen bonds between amino acid residues in the digestion enzymes and EGC. In vitro digestion experiments showed that TPs reduced the extent of starch hydrolysis. The findings of this study contribute to the theoretical understanding and provide a foundation for combating human health issues by elucidating the effects of TPs on the starch digestion process. The knowledge gained from this research has implications for developing strategies to enhance the health-promoting properties of tea and its potential application in preventing or managing metabolic disorders.",
author = "Jinchuan Xu and Andreas Blennow and Xingxun Liu and Shujun Wang",
year = "2023",
doi = "10.1021/acsfoodscitech.3c00192",
language = "English",
volume = "3",
pages = "1532--1539",
journal = "ACS Food Science & Technology",
issn = "2692-1944",
publisher = "ACS Publications",
number = "9",

}

RIS

TY - JOUR

T1 - Binding of Specific Tea Polyphenols to Hydrolytic Enzymes and Their Inhibitory Effects on Oat Starch Digestion

AU - Xu, Jinchuan

AU - Blennow, Andreas

AU - Liu, Xingxun

AU - Wang, Shujun

PY - 2023

Y1 - 2023

N2 - The purpose of this study was to investigate the effects of tea polyphenols (TPs) on the activity of starch digestion enzymes, including α-amylase, pancreatin, and amyloglucosidase (AMG), which simulate the digestion process in the oral cavity, stomach, and small intestine, respectively. We determined the main polyphenol composition of green tea polyphenols using high-performance liquid chromatography (HPLC), with a focus on epicatechin (EC), epigallocatechin (EGC), epigallocatechin gallate (EGCG), and epicatechin gallate (ECG). When mixed with hydrolytic enzymes, the fluorescence emission spectra data revealed a significant decrease in the fluorescence intensity of TPs over time, indicating an increased interaction between TPs and the hydrolytic enzymes with increasing TPs concentration within the measured range. The inhibition percentage (%) and fluorescence emission spectral data demonstrated an initial increase in the inhibition of TPs with increasing concentration, followed by a plateau. Moreover, molecular docking studies revealed that EGC exhibited a higher affinity than did the other catechins, resulting in the formation of more hydrogen bonds between amino acid residues in the digestion enzymes and EGC. In vitro digestion experiments showed that TPs reduced the extent of starch hydrolysis. The findings of this study contribute to the theoretical understanding and provide a foundation for combating human health issues by elucidating the effects of TPs on the starch digestion process. The knowledge gained from this research has implications for developing strategies to enhance the health-promoting properties of tea and its potential application in preventing or managing metabolic disorders.

AB - The purpose of this study was to investigate the effects of tea polyphenols (TPs) on the activity of starch digestion enzymes, including α-amylase, pancreatin, and amyloglucosidase (AMG), which simulate the digestion process in the oral cavity, stomach, and small intestine, respectively. We determined the main polyphenol composition of green tea polyphenols using high-performance liquid chromatography (HPLC), with a focus on epicatechin (EC), epigallocatechin (EGC), epigallocatechin gallate (EGCG), and epicatechin gallate (ECG). When mixed with hydrolytic enzymes, the fluorescence emission spectra data revealed a significant decrease in the fluorescence intensity of TPs over time, indicating an increased interaction between TPs and the hydrolytic enzymes with increasing TPs concentration within the measured range. The inhibition percentage (%) and fluorescence emission spectral data demonstrated an initial increase in the inhibition of TPs with increasing concentration, followed by a plateau. Moreover, molecular docking studies revealed that EGC exhibited a higher affinity than did the other catechins, resulting in the formation of more hydrogen bonds between amino acid residues in the digestion enzymes and EGC. In vitro digestion experiments showed that TPs reduced the extent of starch hydrolysis. The findings of this study contribute to the theoretical understanding and provide a foundation for combating human health issues by elucidating the effects of TPs on the starch digestion process. The knowledge gained from this research has implications for developing strategies to enhance the health-promoting properties of tea and its potential application in preventing or managing metabolic disorders.

U2 - 10.1021/acsfoodscitech.3c00192

DO - 10.1021/acsfoodscitech.3c00192

M3 - Journal article

VL - 3

SP - 1532

EP - 1539

JO - ACS Food Science & Technology

JF - ACS Food Science & Technology

SN - 2692-1944

IS - 9

ER -

ID: 363265072