Phenolics from Sterculia nobilis Smith pericarp by-products delay carbohydrate digestion by uncompetitively inhibiting α-glucosidase and α-amylase

Yang, Yujiao; Zhang, Pingling; Huang, Zhe; Zhao, Zhengang

doi:10.1016/j.lwt.2022.114339

Cited by 20 publications

(8 citation statements)

References 42 publications

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“…All lines passed through the coordinate origin (0, 0) and the slopes of the lines were decreased with the increasing concentrations of rugosin C ethyl ester. These findings suggested that rugosin C ethyl ester acted as a reversible inhibitor, diminishing the activity of α‐glucosidase (Yang et al ., 2023).…”

Section: Resultsmentioning

confidence: 99%

Discovery of a new tannin compound as an α‐glucosidase inhibitor from Carya cathayensis Sarg. kernels and its inhibitory kinetics

Zhao,

Chen,

Liu

et al. 2024

Int J of Food Sci Tech

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SummaryInhibition of α‐glucosidases is recognised as an effective approach towards managing postprandial hyperglycaemia. This study aimed to identify a specific compound in Carya cathayensis Sarg. kernels (CCSKs) exhibiting strong inhibitory activities against α‐glucosidase and elucidate the inhibitory kinetic mechanism. Employing a bioassay‐guided approach, an α‐glucosidase inhibitor was isolated from CCSKs through sequential chromatography protocol involving AB‐8 macroporous adsorptive resin, Sephadex LH‐20 and C18‐reversed phase silica gel. The resulting inhibitor was a novel tannin compound, identified as rugosin C ethyl ester. Rugosin C ethyl ester displayed superior inhibitory activity (IC50 of 2.60 μg/mL) compared to acarbose (IC50 of 105.95 μg/mL). The kinetic analysis indicated that rugosin C ethyl ester had a mixed‐type reversible inhibition against α‐glucosidase. The inhibition constants (Ki and Kis) were determined to be 3.119 and 0.856 μg/mL, respectively. The findings indicated that rugosin C ethyl ester might serve as a promising functional ingredient in low‐glycemic index foods.

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Section: Resultsmentioning

confidence: 99%

Discovery of a new tannin compound as an α‐glucosidase inhibitor from Carya cathayensis Sarg. kernels and its inhibitory kinetics

Zhao,

Chen,

Liu

et al. 2024

Int J of Food Sci Tech

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“…The α‐amylase inhibition assay was conducted in accordance with a previously reported protocol, with minor modifications (Yang et al ., 2023). The sample was divided into four groups: the sample group contained 0.05 mL of α‐amylase (2 U/mL) and 0.05 mL of the test sample; the sample control group contained 0.05 mL of the test sample and phosphate‐buffered saline (PBS); the control group contained 0.05 mL of α‐amylase (2 U/mL) and 0.05 mL of PBS, while the blank group consisted solely of PBS.…”

Section: Methodsmentioning

confidence: 99%

Exploring antioxidant activities and inhibitory effects against α‐amylase and α‐glucosidase of Elaeocarpus braceanus fruits: insights into mechanisms by molecular docking and molecular dynamics

Li,

Zhang,

Liu

et al. 2023

Int J of Food Sci Tech

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SummaryThe present work investigated the antioxidant activity and inhibitory effects towards α‐amylase and α‐glucosidase of phenolic compounds in Elaeocarpus braceanus fruits and clarified their possible mechanisms based on molecular docking and dynamic analysis. A total of 12 phenolic compounds were identified and quantified in the extracts of E. braceanus fruits using UHPLC‐ESI‐HRMS/MS. The TPC and TFC were 229.18 ± 5.76 mg GAE/g and 144.85 ± 1.17 mg RE/g, respectively. In vitro analyses, E. braceanus fruits extracts exhibited good antioxidant activities and demonstrated strong inhibitory effects towards α‐amylase and α‐glucosidase. Molecular docking and molecular dynamics results showed that quercetin and myricetin can stably form hydrogen bonds and van der Waals forces with the active amino acid residues of α‐amylase and α‐glucosidase, and thereby inhibiting their enzymatic activities. The findings might provide a good potential natural resource for improving oxidative stress damage and controlling blood glucose in diabetes.

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“…It is commonly native to Vietnam, Indonesia, Japan, and south China and is usually utilized to heal gastrointestinal and circulatory problems [ 113 , 114 , 115 ]. The dark red shell of S. nobilis Smith fruit (pericarp) has been investigated for its inhibition activity against digestive enzymes [ 103 ]. The study showed that the pericarp ethyl acetate fraction has a potent uncompetitive α-amylase activity, with an IC 50 of 13.55 μg/mL against 19.45 μg/mL for acarbose.…”

Section: Plant Extracts As An α-Amylase Inhibitor Sourcementioning

confidence: 99%

“…The study showed that the pericarp ethyl acetate fraction has a potent uncompetitive α-amylase activity, with an IC 50 of 13.55 μg/mL against 19.45 μg/mL for acarbose. Spectroscopic methods were used to elaborate the mechanism of α-amylase inhibition, and the results showed the ethyl acetate fraction alters the enzyme’s secondary structure and tryptophan/tyrosine residue microenvironment, resulting in enzyme activity inhibition [ 103 ]. The early investigation of these traditional medicinal plant extracts demonstrated promising α-amylase inhibitory activity, but more research is needed to confirm their anti-diabetic impact.…”

Section: Plant Extracts As An α-Amylase Inhibitor Sourcementioning

confidence: 99%

New Insights into the Latest Advancement in α-Amylase Inhibitors of Plant Origin with Anti-Diabetic Effects

Kashtoh

Baek

2023

Plants

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The rising predominance of type 2 diabetes, combined with the poor medical effects seen with commercially available anti-diabetic medications, has motivated the development of innovative treatment approaches for regulating postprandial glucose levels. Natural carbohydrate digestion enzyme inhibitors might be a viable option for blocking dietary carbohydrate absorption with fewer side effects than manufactured medicines. Alpha-amylase is a metalloenzyme that facilitates digestion by breaking down polysaccharides into smaller molecules such as maltose and maltotriose. It also contributes to elevated blood glucose levels and postprandial hyperglycemia. As a result, scientists are being urged to target α-amylase and create inhibitors that can slow down the release of glucose from carbohydrate chains and prolong its absorption, thereby resulting in lower postprandial plasma glucose levels. Natural α-amylase inhibitors derived from plants have gained popularity as safe and cost-effective alternatives. The bioactive components responsible for the inhibitory actions of various plant extracts have been identified through phytochemical research, paving the way for further development and application. The majority of the findings, however, are based on in vitro investigations. Only a few animal experiments and very few human investigations have confirmed these findings. Despite some promising results, additional investigation is needed to develop feasible anti-diabetic drugs based on plant-derived pancreatic α-amylase inhibitors. This review summarizes the most recent findings from research on plant-derived pancreatic α-amylase inhibitors, including plant extracts and plant-derived bioactive compounds. Furthermore, it offers insights into the structural aspects of the crucial therapeutic target, α-amylases, in addition to their interactions with inhibitors.

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Phenolics from Sterculia nobilis Smith pericarp by-products delay carbohydrate digestion by uncompetitively inhibiting α-glucosidase and α-amylase

Cited by 20 publications

References 42 publications

Discovery of a new tannin compound as an α‐glucosidase inhibitor from Carya cathayensis Sarg. kernels and its inhibitory kinetics

Discovery of a new tannin compound as an α‐glucosidase inhibitor from Carya cathayensis Sarg. kernels and its inhibitory kinetics

Exploring antioxidant activities and inhibitory effects against α‐amylase and α‐glucosidase of Elaeocarpus braceanus fruits: insights into mechanisms by molecular docking and molecular dynamics

New Insights into the Latest Advancement in α-Amylase Inhibitors of Plant Origin with Anti-Diabetic Effects

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