Evaluation of α-glucosidase inhibition potential of some flavonoids from Epimedium brevicornum

Phan, Minh Anh Thu; Jin, Wang; Tang, Jingyi; Lee, Yan Zhi; Ng, Ken

doi:10.1016/j.lwt.2013.04.002

Cited by 114 publications

(71 citation statements)

References 39 publications

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“…The kaempferol and acarbose concentrations leading to a loss of 50% enzyme activity (IC 50 ) were calculated to be (1.16 ± 0.04) Â 10 À5 and (2.09 ± 0.03) Â 10 À4 mol L À1 (n = 3), respectively, indicating that kaempferol showed a much better inhibitory ability on a-glucosidase than acarbose. The IC 50 value of kaempferol determined in the present study for yeast a-glucosidase was consistent with earlier report (IC 50 = 1.86 Â 10 À5 mol L À1 ) (Phan et al, 2013). As reported previously, flavonoids quercetin and myricetin with a similar structure as kaempferol exhibited different inhibition effects on a-glucosidase: myricetin (3 0 , 4 0 , 5 0 -OH) > quercetin (3 0 , 4 0 -OH) > kaempferol (4 0 -OH) (Tadera, Minami, Takamatsu, & Matsuoka, 2006).…”

Section: Analysis Of Inhibitory Kineticssupporting

confidence: 93%

“…3C, all the data lines on the Lineweaver-Burk plots intersected in the second quadrant, indicating that kaempferol induced a mixed-type of inhibition, which was consistent with a previous report (Phan et al, 2013). From the Eqs.…”

Section: Kinetic Type Of Inhibitionsupporting

confidence: 91%

“…In recent years, kaempferol extracted from guava leaves has been reported to show a potent inhibitory activity on a-glucosidase with IC 50 value of 5.2 Â 10 À6 mol L À1 . It exhibited much stronger a-glucosidase inhibitory activity than acarbose with 95.1% inhibition (Phan, Wang, Tang, Lee, & Ng, 2013). However, to our knowledge, the study was limited to the enzymatic activity assay, and no report is available on the inhibition mechanism of kaempferol on a-glucosidase.…”

Section: Introductionmentioning

confidence: 99%

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Inhibitory kinetics and mechanism of kaempferol on α-glucosidase

et al. 2016

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Section: Analysis Of Inhibitory Kineticssupporting

confidence: 93%

Section: Kinetic Type Of Inhibitionsupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

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Inhibitory kinetics and mechanism of kaempferol on α-glucosidase

et al. 2016

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“…α-Glucosidase inhibitory activity was evaluated as previously described by Phan et al (2013) with modifications. For this, 50 µl of test sample (in 50 g/100 ml DMSO) was mixed with 50 µl of potassium phosphate buffer (50 mM, pH 6.8) prior to the addition of 100 µl of yeast α-glucosidase (0.2 U/ml; Sigma Chemical Co.).…”

Section: Food Technology and Economy Engineering And Physical Propermentioning

confidence: 99%

Production and characterisation of alcohol-insoluble dietary fibre as a potential sourcefor functional carbohydrates produced by enzymatic depolymerisation of buckwheat hulls

HeeJin¹,

Kyung-Young²

2015

Czech J. Food Sci.

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Im H.J., Yoon K.Y. (2015): Production and characterisation of alcohol-insoluble dietary fibre as a potential source for functional carbohydrates produced by enzymatic depolymerisation of buckwheat hulls. Czech J. Food Sci., 33: 449-457.We examined the potential use of buckwheat hulls as a raw material for producing soluble dietary fibre. The insoluble fibre fraction obtained from buckwheat hulls was hydrolysed by two commercial enzymes (Celluclast 1.5L for the cellulose fraction and Viscozyme L for the hemicellulose fraction) to obtain soluble fibre hydrolysates. Alcohol-insoluble dietary fibre (AIF) was separated from the freeze-dried soluble hydrolysate by treatment with 85% ethanol. The waterholding, oil-binding, and swelling capacities of AIF were increased by enzymatic hydrolysis. AIF had significantly (P < 0.05) higher functional properties than the control. AIF from the hemicellulose fraction effectively hindered the diffusion of glucose and bile acid from dialysis membranes, and had a significantly (P < 0.05) greater bile acid inhibitory effect than carboxymethylcellulose or pectin. It can be concluded that AIF from buckwheat hulls by enzymatic hydrolysis can used as dietary supplement and additive in the food industry.

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“…It was reported that the α-glucosidase inhibitory activity of phenolics is affected by their chemical structure (De melo et al, 2006). The formation/degradation of large polymeric phenolics and the degradation of small phenolics during fermentation may increase or decrease the α-glucosidase inhibitory activity (Yang et al, 2012;You et al, 2012;Phan et al, 2013). In addition, some studies reported that the production of acidic metabolites by lactic bacteria may further enhance the α-glucosidase inhibitory activity (AposToliDis et al, 2007;Ankolekar et al, 2012).…”

Section: Changes In α-Glucosidase Inhibitory Activity During Fermentamentioning

confidence: 99%

Changes of anti-glucosidase content and some other characteristics in mulberry juice during fermentation withLeuconostoc mesenteroides

Zheng¹,

Yu²,

Xiao³

et al. 2014

Acta Alimentaria

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Changes in microbial population, pH, sugar, organic acid, anthocyanins, total soluble phenolics, and anti-glucosidase contents were measured during fermentation of mulberry juice at 30 °C by probiotic Leuconostoc mesenteroides showing rapid growth after an approximately 1-day lag phase and reaching a maximum of 8.6 log CFU ml -1 after 4 d. During the rapid growth phase, the main mulberry juice sugars, glucose and fructose, were largely consumed, and the acidic metabolites, lactic acid and acetic acid, were produced accordingly. A slow decrease in the concentration of the main organic acid, citric acid, was also observed during fermentation. After 4 d fermentation, anthocyanin content showed a 44.4% reduction, but the total amount of soluble phenolics and α-glucosidase inhibitory activity showed no significant changes (P>0.05). This suggests that L. mesenteroides fermentation of mulberry juice is a good strategy to enhance its probiotic value and to decrease the sugar content without changing the anti-glucosidase activity, which is required to reduce postprandial rise in blood glucose.

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Evaluation of α-glucosidase inhibition potential of some flavonoids from Epimedium brevicornum

Cited by 114 publications

References 39 publications

Inhibitory kinetics and mechanism of kaempferol on α-glucosidase

Inhibitory kinetics and mechanism of kaempferol on α-glucosidase

Production and characterisation of alcohol-insoluble dietary fibre as a potential sourcefor functional carbohydrates produced by enzymatic depolymerisation of buckwheat hulls

Changes of anti-glucosidase content and some other characteristics in mulberry juice during fermentation withLeuconostoc mesenteroides

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