Inhibitory activity of flavonoids against human sucrase-isomaltase (α-glucosidase) activity in a Caco-2/TC7 cellular model

2022 ◽  
Author(s):  
Carina Proença ◽  
Ana T. Rufino ◽  
José Miguel P. Ferreira de Oliveira ◽  
Marisa Freitas ◽  
Pedro A. Fernandes ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Cellular Model ◽  
Oh Groups ◽  
Glucosidase Activity

Flavonoids may be effective inhibitors of SI in Caco-2/TC7 cells when using natural substrates maltose and sucrose. The chemical features that favor the SI inhibition by flavonoids are the presence of –OH groups at C-3, C-3′, C-4′, C-7 and C-8.

scholarly journals Suppressing the oxidation of LDL and DNA strand breakage of bioactives in dehulled and hull fraction of lentils

2020 ◽  
Vol 12 ◽  
Author(s):  
JuDong Yeo ◽  
Fereidoon Shahidi
Keyword(s):  
Seed Coat ◽  
Inhibitory Activity ◽  
Plant Cells ◽  
Glucosidase Activity ◽  
Parenchyma Cells ◽  
Strand Breakage ◽  
Inhibitory Activities ◽  
Dna Strand ◽  
Bound Phenolics ◽  
Dna Strand Breakage

Hull/seed coat contains various plant cells that are responsible for sustaining the life of seeds in which phenolics perform significant roles in supporting their functions. In the present study, inhibitory activities against the oxidation of LDL and DNA of soluble- and insoluble-bound phenolics in the dehulled and hull fractions of lentils were determined. In addition, their α-glucosidase inhibitory activity was also assessed. The hulls possessed much higher levels of phenolics in both the soluble- and insoluble-bound forms than dehulled grain fractions, and this led to their potent activities in suppressing the oxidation of LDL and DNA and inhibiting α-glucosidase activity. The high bioactivities of hulls might be due to the existence of various types of cells such as palisade and parenchyma cells containing numerous phenolics for sustaining their functions. This study may help in a better understanding of the localization of soluble- and insoluble-bound phenolics in the structure of lentil.

scholarly journals Ishophloroglucin A, a Novel Phlorotannin for Standardizing the Anti-α-Glucosidase Activity of Ishige okamurae

Marine Drugs ◽  
2018 ◽  
Vol 16 (11) ◽  
pp. 436 ◽  
Author(s):  
BoMi Ryu ◽  
Yunfei Jiang ◽  
Hyun-Soo Kim ◽  
Jee-Min Hyun ◽  
Sang-Bin Lim ◽  
...  
Keyword(s):  
Analytical Method ◽  
Inhibitory Activity ◽  
Glucosidase Activity ◽  
Ishige Okamurae ◽  
Effective Use

Nutraceutical use of algae requires understanding of the diversity and significance of their active compositions for intended activities. Ishige okamurae (I. okamurae) extract is well-known to possess α-glucosidase inhibitory activity; however, studies are needed to investigate its active composition in order to standardize its α-glucosidase inhibitory activity. In this study, we observed the intensity of the dominant compounds of each I. okamurae extract harvested between 2016 and 2017, and the different potency of each I. okamurae extract against α-glucosidase. By comparing the anti-α-glucosidase ability of the dominant compounds, a novel Ishophloroglucin A with highest α-glucosidase inhibitory activity was identified and suggested for standardization of anti-α-glucosidase activity in I. okamurae extract. Additionally, a validated analytical method for measurement of Ishophloroglucin A for future standardization of I. okamurae extract was established in this study. We suggest using Ishophloroglucin A to standardize anti-α-glucosidase potency of I. okamurae and propose the significance of standardization based on their composition for effective use of algae as marine-derived nutraceuticals.

scholarly journals Inhibition of α-glucosidase activity, metals content, and phytochemical profiling of Andrographis paniculata from different geographical origins based on FTIR and UHPLC-Q-Orbitrap HRMS metabolomics

2021 ◽  
Vol 22 (3) ◽  
Author(s):  
Mohamad Rafi ◽  
DEWI ANGGRAINI SEPTANINGSIH ◽  
ALFI HUDATUL KAROMAH ◽  
LUKMAN LUKMAN ◽  
BAMBANG PRAJOGO ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Geographical Origin ◽  
Raw Materials ◽  
Herbal Medicines ◽  
Water Extract ◽  
Ethanol Extract ◽  
Ftir Spectra ◽  
Andrographis Paniculata ◽  
Active Components ◽  
Glucosidase Activity

Abstract. Rafi M, Septaningsih DA, Karomah AH, Lukman, Prajogo B, Amran MB, Rohman A. 2021. Inhibition of α-glucosidase activity, metals content, and phytochemical profiling of Andrographis paniculata from different geographical origins based on FTIR and UHPLC-Q-Orbitrap HRMS metabolomics. Biodiversitas 22: 1535-1542. Ensuring consistency of quality, safety, and efficacy of herbal medicines from raw materials to finished products is important because of the variability in medicinal plants' active components. One of the plants that have been used as an antidiabetic herbal medicine is A. paniculata. This study aims to determine α-glucosidase inhibitory activity, the content of several metals, FTIR spectrum profile, and putative identification of A. paniculata metabolites using UHPLC-Q-Orbitrap HRMS from different geographical origin. We found that ethanol extract of A. paniculata gave higher inhibition of α-glucosidase activity compared to water extract. Eight metals were determined using FAAS and FAES, and calcium showed the highest content in all A. paniculata samples. FTIR spectra of A. paniculata showed a similar profile and only differed in the absorbance. We detected the presence of OH, C=O, C=C aromatic, and C-O functional groups in A. paniculata extract. About 32 metabolites were putatively identified in A. paniculata, mainly from phenolic and diterpene lactones class compounds based on UHPLC-Q-Orbitrap HRMS. Using a combination of FTIR spectra and peak area from 32 identified peaks, we can clustered A. paniculata based on its geographical origin. Based on the result obtained, the geographical origin of A. paniculata affected the metals and metabolites composition and level, resulting in different levels of α-glucosidase inhibitory activity.

scholarly journals Chemical synthesis, inhibitory activity and molecular mechanism of 1-deoxynojirimycin–chrysin as a potent α-glucosidase inhibitor

RSC Advances ◽  
2021 ◽  
Vol 11 (61) ◽  
pp. 38703-38711
Author(s):  
Ran Zhang ◽  
Yueyue Zhang ◽  
Gaiqun Huang ◽  
Xiangdong Xin ◽  
Liumei Tang ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Chemical Synthesis ◽  
Molecular Mechanism ◽  
Inhibitory Activity ◽  
Effective Strategy ◽  
Glucosidase Inhibitor ◽  
Glucosidase Activity

Hyperglycemia can be efficaciously regulated by inhibiting α-glucosidase activity and this is regarded as an effective strategy to treat type 2 diabetes.

scholarly journals Flavanol Polymerization Is a Superior Predictor of α-Glucosidase Inhibitory Activity Compared to Flavanol or Total Polyphenol Concentrations in Cocoas Prepared by Variations in Controlled Fermentation and Roasting of the Same Raw Cocoa Beans

Antioxidants ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 635 ◽  
Author(s):  
Kathryn C. Racine ◽  
Brian D. Wiersema ◽  
Laura E. Griffin ◽  
Lauren A. Essenmacher ◽  
Andrew H. Lee ◽  
...  
Keyword(s):  
Negative Correlation ◽  
Inhibitory Activity ◽  
Cocoa Beans ◽  
Strong Negative Correlation ◽  
Total Polyphenol ◽  
Cocoa Powder ◽  
Glucosidase Activity

Raw cocoa beans were processed to produce cocoa powders with different combinations of fermentation (unfermented, cool, or hot) and roasting (not roasted, cool, or hot). Cocoa powder extracts were characterized and assessed for α-glucosidase inhibitory activity in vitro. Cocoa processing (fermentation/roasting) contributed to significant losses of native flavanols. All of the treatments dose-dependently inhibited α-glucosidase activity, with cool fermented/cool roasted powder exhibiting the greatest potency (IC50: 68.09 µg/mL), when compared to acarbose (IC50: 133.22 µg/mL). A strong negative correlation was observed between flavanol mDP and IC50, suggesting flavanol polymerization as a marker of enhanced α-glucosidase inhibition in cocoa. Our data demonstrate that cocoa powders are potent inhibitors of α-glucosidase. Significant reductions in the total polyphenol and flavanol concentrations induced by processing do not necessarily dictate a reduced capacity for α-glucosidase inhibition, but rather these steps can enhance cocoa bioactivity. Non-traditional compositional markers may be better predictors of enzyme inhibitory activity than cocoa native flavanols.

IN VITRO SCREENING OF ACTINIOPTERIS DICHOTOMA FOR ENZYME INHIBITORY ACTIVITY RELATED TO TYPE 2 DIABETES

INDIAN DRUGS ◽  
2016 ◽  
Vol 53 (06) ◽  
pp. 70-73
Author(s):  
M Telagari ◽  
◽  
K. K. Hullatti
Keyword(s):  
Type 2 Diabetes ◽  
Inhibitory Activity ◽  
Skin Diseases ◽  
In Vitro Screening ◽  
Glucosidase Activity ◽  
Ic50 Values ◽  
Calculated Fraction

Actiniopteris dichotoma Mett. (Pteridaceae) is documented in Ayurveda for treatment of Prameha (Diabetes), Atisara and skin diseases. However, the antidiabetic properties of this plant have not been fully validated using scientific tools. The present study screens the A. dichotoma extract and fractions for enzyme inhibitory (α–amylase and α–glucosidase) activity related to type 2 diabetes. The extract was prepared using cold maceration followed by Soxhlation and finally fractionated the combined extracts. Different concentrations (0.1–0.5 mg/mL) of extract and four fractions were subjected to enzyme inhibitory assays. The absorbance was measured at 540 and 405 nm and IC50 values were calculated. Fraction 2 has shown highest α–amylase and α–glucosidase inhibitory activity, (IC50 values are 0.131 and 0.114 mg/mL) which was comparable with acarbose (0.125 and 0.093 mg/mL). Hence, further studies may throw light on the antidiabetic potential of A. dichotoma especially in the management of T2D.

scholarly journals Bioactivities and ACE-inhibitory peptides releasing potential of lactic acid bacteria in fermented soy milk

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
J. Undhad Trupti ◽  
Sujit Das ◽  
Divyang Solanki ◽  
Dhvany Kinariwala ◽  
Subrota Hati
Keyword(s):  
Proteolytic Activity ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Growth Behavior ◽  
Soy Milk ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Inhibitory Peptides ◽  
Glucosidase Activity ◽  
Ace Inhibitory

Abstract This study was designed to evaluate the bioactivities such as β-glucosidase activity, α-galactosidase activity, and the growth behavior of the Lactobacillus cultures in soy milk medium. Ten Lactobacillus cultures were considered in this study. L. fermentum (M2) and L. casei (NK9) were selected due to their better α-galactosidase, β-glucosidase activity and growth behavior in soy milk medium during fermentation. Further, soy milk fermented with M2 showed higher proteolytic activity (0.67 OD) and ACE-inhibitory (48.44%) than NK9 (proteolytic activity: 0.48 OD and ACE-inhibitory activity: 41.33%). Bioactive peptides produced during the fermentation of soy milk using the selected Lactobacillus cultures were also identified with potent ACE-inhibitory activity by MALDI-TOF spectrometry, and the identified ACE inhibitory peptide sequences from fermented soy milk were characterized using Biopep database. Graphical abstract

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