Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia
The postprandial hyperglycemia of diabetic patients is associated with a-amylase and a-glucosidase, searching safer enzyme inhibitors and deciphering their inhibition mechanism are important. In this study, gallocatechin gallate (GCG) was found to exert strong inhibition on α-amylase and α-glucosida...
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doaj-e8030fd1842c4367afaa08ac42535b232021-04-30T07:14:19ZengElsevierJournal of Functional Foods1756-46462018-09-0148200209Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemiaXiaqing Wu0Huafang Ding1Xing Hu2Junhui Pan3Yijing Liao4Deming Gong5Guowen Zhang6State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Corresponding authors.State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; New Zealand Institute of Natural Medicine Research, 8 Ha Crescent, Auckland 2104, New ZealandState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Corresponding authors.The postprandial hyperglycemia of diabetic patients is associated with a-amylase and a-glucosidase, searching safer enzyme inhibitors and deciphering their inhibition mechanism are important. In this study, gallocatechin gallate (GCG) was found to exert strong inhibition on α-amylase and α-glucosidase in the mixed-type and non-competitive manners, respectively. GCG could bind with α-amylase and α-glucosidase to form the complexes, which induced conformational changes of the two carbohydrate digestive enzymes. Docking analysis verified that GCG interacted with pivotal amino acids within the active site of α-amylase, while it bound to a site close to the active site of α-glucosidase, which might affect active site, causing declines in a-amylase and α-glucosidase activities. Moreover, the combination of GCG with acarbose increased the inhibition of α-amylase and α-glucosidase and reduced the dosage of acarbose. This study may provide theoretical basis for designing novel functional foods of GCG for the prevention and treatment of diabetes.http://www.sciencedirect.com/science/article/pii/S175646461830358XGallocatechin gallateα-Amylaseα-GlucosidaseInhibitory mechanism |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Xiaqing Wu Huafang Ding Xing Hu Junhui Pan Yijing Liao Deming Gong Guowen Zhang |
spellingShingle |
Xiaqing Wu Huafang Ding Xing Hu Junhui Pan Yijing Liao Deming Gong Guowen Zhang Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia Journal of Functional Foods Gallocatechin gallate α-Amylase α-Glucosidase Inhibitory mechanism |
author_facet |
Xiaqing Wu Huafang Ding Xing Hu Junhui Pan Yijing Liao Deming Gong Guowen Zhang |
author_sort |
Xiaqing Wu |
title |
Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia |
title_short |
Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia |
title_full |
Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia |
title_fullStr |
Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia |
title_full_unstemmed |
Exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia |
title_sort |
exploring inhibitory mechanism of gallocatechin gallate on a-amylase and a-glucosidase relevant to postprandial hyperglycemia |
publisher |
Elsevier |
series |
Journal of Functional Foods |
issn |
1756-4646 |
publishDate |
2018-09-01 |
description |
The postprandial hyperglycemia of diabetic patients is associated with a-amylase and a-glucosidase, searching safer enzyme inhibitors and deciphering their inhibition mechanism are important. In this study, gallocatechin gallate (GCG) was found to exert strong inhibition on α-amylase and α-glucosidase in the mixed-type and non-competitive manners, respectively. GCG could bind with α-amylase and α-glucosidase to form the complexes, which induced conformational changes of the two carbohydrate digestive enzymes. Docking analysis verified that GCG interacted with pivotal amino acids within the active site of α-amylase, while it bound to a site close to the active site of α-glucosidase, which might affect active site, causing declines in a-amylase and α-glucosidase activities. Moreover, the combination of GCG with acarbose increased the inhibition of α-amylase and α-glucosidase and reduced the dosage of acarbose. This study may provide theoretical basis for designing novel functional foods of GCG for the prevention and treatment of diabetes. |
topic |
Gallocatechin gallate α-Amylase α-Glucosidase Inhibitory mechanism |
url |
http://www.sciencedirect.com/science/article/pii/S175646461830358X |
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