Different Proportions of Huangqi (Radix Astragali Mongolici) and Honghua (Flos Carthami) Injection onα-Glucosidase andα-Amylase Activities

Objective.To study the effect of different proportions of Huangqi (Radix Astragali Mongolici) and Honghua (Flos Carthami) injection onα-glucosidase andα-amylase activity simultaneously.Methods.The injections were prepared according to the standards of the China Food and Drug Administration. The assay for potentialα-glucosidase inhibitors was based on the hydrolysis of 4-methylumbelliferyl-α-D-glucopyranoside (4-MUG). Theα-amylase EnzChek assay kit was used to determine potentialα-amylase inhibitors. Acarbose was the positive control.Results.The half maximal (50%) inhibitory concentration (IC50) of acarbose againstα-glucosidase andα-amylase was (1.8±0.4)μg/mL and (227±32)μg/mL, respectively. Honghua showed significant inhibition ofα-glucosidase activity compared with Huangqi (P<0.01). Honghua inhibitedα-amylase activity, but Huangqi did not. IC50s forα-glucosidase inhibition by mixtures at 10 : 1, 5 : 1, and 2 : 1 were significantly lower than those at the 20 : 1 mixture (P<0.01).α-Amylase inhibition by the 2 : 1 mixture was significantly higher than that by the 20 : 1, 10 : 1, and 5 : 1 mixtures at 500 μg/mL and 1000 μg/mL (P<0.01), with 5 : 1 significantly higher than 20 : 1 and 10 : 1 at 1000 μg/mL (P<0.01).Conclusion.Honghua significantly inhibitedα-glucosidase activity compared with Huangqi (P<0.01). For simultaneous inhibition ofα-glucosidase andα-amylase activities, the mixtures at 2 : 1 and 5 : 1 exhibited significant effects compared with those at 20 : 1 (P<0.01).

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Screening and structural characterization of potential α-glucosidase inhibitors from Radix Astragali flavonoids extract by ultrafiltration LC-DAD-ESI-MSn

Analytical Methods ◽

10.1039/c4ay02081b ◽

2015 ◽

Vol 7 (1) ◽

pp. 123-128 ◽

Cited By ~ 10

Author(s):

Wenyue Jiang ◽

Hong Kan ◽

Pengdong Li ◽

Shu Liu ◽

Zhongying Liu

Keyword(s):

Diabetes Mellitus ◽

Structural Characterization ◽

Radix Astragali ◽

Glucosidase Activity ◽

Glucosidase Inhibitors

Inhibition of intestinal α-glucosidase activity is one important mechanism for the management of diabetes mellitus (DM).

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β-Glucosidase Activity of Lactiplantibacillus plantarum UNQLp 11 in Different Malolactic Fermentations Conditions: Effect of pH and Ethanol Content

Fermentation ◽

10.3390/fermentation7010022 ◽

2021 ◽

Vol 7 (1) ◽

pp. 22

Author(s):

Natalia S. Brizuela ◽

Marina Arnez-Arancibia ◽

Liliana Semorile ◽

María Ángeles Pozo-Bayón ◽

Bárbara M. Bravo-Ferrada ◽

...

Keyword(s):

Pinot Noir ◽

Gas Chromatography Mass Spectrometry ◽

Red Wines ◽

Ph Values ◽

Glucosidase Activity ◽

Sorptive Extraction ◽

Ethanol Content ◽

Volatile Precursors ◽

Hydrolysis Of ◽

High Ethanol

Lactiplantibacillus plantarum strain UNQLp 11 is a lactic acid bacterium with the potential to carry out malolactic fermentation (MLF) in red wines. Recently, the complete genome of UNQLp 11 was sequenced and this strain possesses four loci of the enzyme β-glucosidase. In order to demonstrate that these glucosidase enzymes could be functional under harsh wine conditions, we evaluated the hydrolysis of p-nitrophenyl-β-D-glucopyranoside (p-NPG) in synthetic wine with different ethanol contents (0%, 12%, and 14% v/v) and at different pH values (3.2, 3.5, and 3.8). Then, the hydrolysis of precursor n-octyl β-D-glucopyranoside was analyzed in sterile Pinot Noir wine (containing 14.5% v/v of ethanol, at different pH values) by headspace sorptive extraction gas chromatography-mass spectrometry (HSSE-GC/MS). The hydrolysis of p-NPG showed that β-glucosidase activity is very susceptible to low pH but induced in the presence of high ethanol content. Furthermore, UNQLp 11 was able to release the glycosilated precursor n-octyl, during MLF to a greater extent than a commercial enzyme. In conclusion, UNQLp 11 could improve the aromatic profile of the wine by the release of volatile precursors during MLF.

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Uji Bioaktivitas Antibakteri Senyawa murni dari Jamur Endofit Sporothrix sp Terhadap Bakteri Escherichia coli dan Staphylococcus aureus

Dinamika Lingkungan Indonesia ◽

10.31258/dli.6.1.p.37-44 ◽

2019 ◽

Vol 6 (1) ◽

pp. 37

Author(s):

Dewi Yudiana Shinta ◽

Yusmarini Yusmarini ◽

Herix Sonata MS ◽

Hilwan Yuda Teruna ◽

Saryono Saryono

Keyword(s):

Escherichia Coli ◽

Staphylococcus Aureus ◽

Endophytic Fungi ◽

Positive Control ◽

Significant Inhibition ◽

New Drugs ◽

Diffusion Method ◽

Significant Difference ◽

Pure Compounds ◽

Escherichia Coli Bacteria

Modern medicines that are developing now come from active ingredients isolated from plants that require large amounts of plants. The development of new drugs from endophytic fungi found obstacles in the amount of pure compounds produced. Therefore further research is needed by using endophytic fungi as a new antimicrobial producer. This study aims to see the ability or activity of pure compounds produced by Sporothrix sp endophytic fungi from Dahlia tuber (Dahlia variabilis). Test the activity of pure compounds produced by Sporothrix sp. Endophytic fungi on E. coli and Staphylococcus aureus determined by disc diffusion method. With doses of 10, 30 and 50μg/disk. In Escherichia coli bacteria doses 10 and 50μg/disk gave significant inhibition of pure compounds from isolation compared to the positive control of ciprofloxacin, which was marked by a statistically significant test result (p <0.05). In contrast to Staphylococcus aureus there was no significant difference in doses of both doses of 10.30 and 50μg/disk. Determination of pure compounds was carried out by HPLC and Infra Red Spectrophotometry.

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Inhibition of intestinal α-glucosidase activity and postprandial hyperglycemia by α-glucosidase inhibitors in fa/fa rats

Nutrition Research ◽

10.1016/s0271-5317(05)80396-3 ◽

1991 ◽

Vol 11 (9) ◽

pp. 1035-1046 ◽

Cited By ~ 17

Author(s):

Zecharia Madar ◽

Ziv Omursky

Keyword(s):

Postprandial Hyperglycemia ◽

Glucosidase Activity ◽

Glucosidase Inhibitors

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An experiment in enzyme evolution studies with Pseudomonas aeruginosa amidase

Bioscience Reports ◽

10.1007/bf01116455 ◽

1988 ◽

Vol 8 (2) ◽

pp. 103-120 ◽

Cited By ~ 16

Author(s):

Patricia H. Clarke ◽

Robert Drew

Keyword(s):

Pseudomonas Aeruginosa ◽

Control System ◽

Experimental Evolution ◽

Positive Control ◽

Enzyme Evolution ◽

Regulator Protein ◽

Hydrolysis Of

The regulation of amidase synthesis in P. aeruginosa is under positive control. This review describes the experimental evolution of amidase and its regulator protein for the hydrolysis of novel substrates and experiments to elucidate the mechanism of the control system.

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New α-Glucosidase inhibitors from the resins of Boswellia species with structure–glucosidase activity and molecular docking studies

Bioorganic Chemistry ◽

10.1016/j.bioorg.2018.04.020 ◽

2018 ◽

Vol 79 ◽

pp. 27-33 ◽

Cited By ~ 13

Author(s):

Najeeb Ur. Rehman ◽

Ajmal Khan ◽

Ahmed Al-Harrasi ◽

Hidayat Hussain ◽

Abdul Wadood ◽

...

Keyword(s):

Molecular Docking ◽

Docking Studies ◽

Molecular Docking Studies ◽

Glucosidase Activity ◽

Glucosidase Inhibitors

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Inhibition of α-Glucosidase, Intestinal Glucose Absorption, and Antidiabetic Properties by Caralluma europaea

Evidence-based Complementary and Alternative Medicine ◽

10.1155/2018/9589472 ◽

2018 ◽

Vol 2018 ◽

pp. 1-8 ◽

Cited By ~ 5

Author(s):

Hayat Ouassou ◽

Touda Zahidi ◽

Saliha Bouknana ◽

Mohamed Bouhrim ◽

Hassane Mekhfi ◽

...

Keyword(s):

Ethyl Acetate Fraction ◽

Inhibitory Effect ◽

Tolerance Test ◽

Glucose Absorption ◽

Significant Inhibition ◽

Oral Glucose ◽

Glucosidase Activity ◽

Intestinal Glucose Absorption

Many medicinal plants around the world are used for therapeutic purposes against several diseases, including diabetes mellitus. Due to their composition of natural substances that are effective and do not represent side effects for users, unlike synthetic drugs, in this study, we investigated the inhibitory effect of Caralluma europaea (CE) on α-glucosidase activity in vitro; then the kinetics of the enzyme were studied with increasing concentrations of sucrose in order to determine the inhibition type of the enzyme. In addition, this effect of Caralluma europaea (CE) was confirmed in vivo using rats as an experimental animal model. Among the five fractions of CE, only the ethyl acetate fraction of C. europaea (EACe) induced a significant inhibition of α-glucosidase and its inhibition mode was competitive. The in vivo studies were conducted on mice and rats using glucose and sucrose as a substrate, respectively, to determine the oral glucose tolerance test (OGTT). The results obtained showed that the EACe and the aqueous extract of C. europaea (AECe) have significantly reduced the postprandial hyperglycemia after sucrose and glucose loading in normal and diabetic rats. AECe, also, significantly decreased intestinal glucose absorption, in situ. The results obtained showed that Caralluma europaea has a significant antihyperglycemic activity, which could be due to the inhibition of α-glucosidase activity and enteric absorption of glucose.

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SOME OBSERVATIONS ON THE PANCREATIC AMYLASE AND INTESTINAL MALTASE OF THE CHICK

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y63-238 ◽

1963 ◽

Vol 41 (1) ◽

pp. 2107-2121 ◽

Cited By ~ 6

Author(s):

B. M. Laws ◽

J. H. Moore

Keyword(s):

Small Intestine ◽

Amylase Activity ◽

Pancreatic Amylase ◽

Ph Optimum ◽

Modified Method ◽

Mucosal Cells ◽

Small Intestinal ◽

The Stability ◽

Hydrolysis Of

The digestive enzymes amylase and maltase were studied in acetone-dried powders or homogenates of the pancreatic and small intestinal tissues and small intestinal contents obtained from chicks of various ages. The stability of pancreatic amylase, which was relatively low in 0.15 M sodium chloride, was increased markedly by the presence of 0.02 M barbiturate buffer. The pH optimum of pancreatic amylase (chloride-activated) was 7.0 whereas that of intestinal maltase was 6.9. High levels of pancreatic amylase activity were found in the newly-hatched chick but these levels decreased during the following 20 days and then remained constant. The contrast between the high amylase and low maltase activities in the contents of the small intestine suggested that molecules of maltose, formed by the hydrolysis of starch, were absorbed as such by the mucosal cells. It appeared that maltose could be absorbed with equal facility from all sections of the small intestine of the 10-day-old chick but in the older birds maltose absorption seemed to occur more readily from the upper small intestine than from the duodenum and lower small intestine. A modified method for the determination of maltase activity is described.

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