Inhibition of α-amylase and α-glucosidase activities by ethanolic extract of Telfairia occidentalis (fluted pumpkin) leaf

Oboh, Ganiyu; Akinyemi, Ayodele Jacob; Ademiluyi, Adedayo O.

doi:10.1016/s2221-1691(12)60219-6

Cited by 55 publications

(30 citation statements)

References 29 publications

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“…Inhibition properties of phenolic compounds against several enzymes have been reported and these studies are mostly limited to digestive and metabolic enzymes such as pepsin, trypsin, α ‐amylase, lipase, and α ‐glucosidase . However, the effects of polyphenols on the activities of enzymes that are important in food technology have rarely been studied to date …”

Section: Introductionsupporting

confidence: 43%

Binding characteristics of polyphenols as milk plasmin inhibitors

Yildirim-Elikoğlu

Vural

2019

J Sci Food Agric

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BACKGROUND The potential use of polyphenols to improve the functional characteristics of dairy products has gained much attention. However, the effects of the polyphenols on naturally occurring enzymes in milk have not been studied extensively. Excess plasmin activity in dairy products might result in several quality defects. The objective of this study was to assess the ability of polyphenols to inhibit plasmin in milk using a molecular and kinetic approach. RESULTS Epicatechin gallate (ECG), epigallocatechin gallate (EGCG), quercetin (QUER), and myricetin (MYR) caused a significant decrease in plasmin activity by 60, 86, 65, and 90%, respectively. The inhibition rates were alleviated in the presence of milk proteins. EGCG, QUER, and MYR, exhibited noncompetitive inhibition against plasmin, whereas ECG caused a mixed‐type inhibition. A decrease in the random structure of plasmin upon the complex formation with ECG, EGCG, QUER, and MYR was found. The other phenolics that were evaluated did not cause any significant changes in plasmin conformation. The observed inhibitory phenolic‐plasmin interactions were dominated by H‐bonds and electrostatic attractions. Green tea extract (GTE) rich in catechins also inhibited plasmin activity in the milk. CONCLUSION Significant changes in the secondary structure of plasmin upon binding of ECG, EGCG, QUER, and MYR led to diminished plasmin activity both in the absence and presence of milk proteins. These flavonoids with promising plasmin inhibitory potential could be used in new dairy formulations leading to controlled undesired consequences of plasmin activity. © 2019 Society of Chemical Industry

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Section: Introductionsupporting

confidence: 43%

Binding characteristics of polyphenols as milk plasmin inhibitors

Yildirim-Elikoğlu

Vural

2019

J Sci Food Agric

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“…These results are in agreement with previous reports which indicated that excessive inhibition of Citation: Kumar PM, Suba V, Reddy RB, Babu SP (2017) Inhibitory Effects of Oncoba Spinosa on Key Enzymes Related to Diabetes Mellitus (α-pancreatic α-amylase could result in the abnormal bacterial fermentation of undigested carbohydrates in the colon and eventually flatulence, abdominal distension and diarrhoea. Thus, stronger inhibition of α-glucosidase activity and mild inhibition of α-amylase activity could address the major drawback of currently used hypoglycaemic drugs [14,15]. The results of the present study showed that OS crude ethanolic extract showed highest pancreatic lipase inhibitory activity in a dose dependent manner when compared to other extracts studied.…”

Section: Discussionmentioning

confidence: 53%

Inhibitory Effects of Oncoba spinosa on Key Enzymes Related to Diabetes Mellitus (A-Amylase and A-Glucosidase) and Obesity (Pancreatic Lipase) in Vitro

M¹,

Suba²,

B³

et al. 2017

J Diabetes Metab

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Aim and Objective: Oncoba spinosa Forssk. (Flacourtiaceae) (OS) is traditionally used for the management of diabetes mellitus. In previous studies, we studied the effect of OS on α-amylase and α-glucosidase inhibition, however the effect of OS on pancreatic lipase inhibition and kinetics of α-amylase, α-glucosidase and pancreatic lipase inhibition were not studied. This study determined the in vitro inhibitory effects of OS against pancreatic lipase and characterized the kinetics of α-amylase, α-glucosidase and pancreatic lipase inhibition. Materials and Methods:Dried powdered roots were successively extracted with various solvents such as petroleum ether, chloroform, ethyl acetate, and 70% ethanol. The successive extracts obtained (62.5-1000 μg/ml) were subjected to in vitro pancreatic lipase inhibitory assay and the most active extract was selected for kinetic studies.Results: Of all the successive extracts studied, the ethanolic extract showed highest pancreatic lipase inhibitory activity. The ethanolic extract showed mixed type of inhibition against α-amylase and pancreatic lipase whereas noncompetitive inhibition against α-glucosidase. Conclusion:The data of this study suggests that OS inhibits amylase, glucosidase and lipase activities, which leads to a reduction in the intestinal absorption of carbohydrates and lipids.

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“…Alpha-amylase and alpha-glucosidase inhibitors delay the action of α-amylase and α-glucosidase to digest carbohydrate and prolong overall carbohydrate digestion time thereby lowering the absorption of (Oboh et al, 2012). In individuals with normal or impaired glucose tolerance with hyperinsulinemia, these inhibitors decrease this condition and improve insulin sensitivity (Lebovittz, 2010).…”

Section: Discussionmentioning

confidence: 99%

“…α-Glucosidase inhibitors like acarbose, miglitol and voglibose are used in conjunction with other antidiabetic drugs, but these inhibitors have been found to possess side effects like flatulence and diarrhoea (Oboh et al, 2012). As a result of this, researchers have grown interest in discovering new and effective α-amylase and α-glucosidase inhibitors with minimal side effects from medicinal plant with known and scientifically proven antidiabetic properties (Onal et al, 2005;Kwon et al, 2008;Shai et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Inhibitory potential of <i>Gossypium arboreum</i> leaf extracts on diabetes key enzymes, α-amylase and α-glucosidase

Kazeem

Abimbola

Ashafa

2013

Bangladesh J Pharmacol

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One of the antidiabetic therapeutic approaches is the reduction in gastrointestinal glucose production and absorption by inhibiting carbohydrate hydrolyzing enzymes such as α-amylase and α-glucosidase. This present study evaluated the α-amylase and α-glucosidase inhibitory potential of the aqueous, ethanolic and acetone leaf extracts of Gossypium arboreum and to further determine the mode of inhibition of the enzymes using kinetic analysis. The aqueous and acetone extract exhibited potent α-amylase and α-glucosidase inhibitory activity with IC50 value of 10.10 mg/mL and 2.75 mg/ mL respectively. These extracts are likely to contain non-competitive inhibitors of both enzymes with reduced Vmax values. The extracts were also found to contain phytochemicals such as tannins and steroids which may be responsible for the inhibitory effect. The results show that the aqueous and acetone extracts of G. arboreum leaf inhibited both α-amylase and α-glucosidase at relatively low concentrations and this could be the reason why the species is employed in the management of blood sugar related disorders by reasonable populations in Nigeria.

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Inhibition of α-amylase and α-glucosidase activities by ethanolic extract of Telfairia occidentalis (fluted pumpkin) leaf

Cited by 55 publications

References 29 publications

Binding characteristics of polyphenols as milk plasmin inhibitors

Binding characteristics of polyphenols as milk plasmin inhibitors

Inhibitory Effects of Oncoba spinosa on Key Enzymes Related to Diabetes Mellitus (A-Amylase and A-Glucosidase) and Obesity (Pancreatic Lipase) in Vitro

Inhibitory potential of <i>Gossypium arboreum</i> leaf extracts on diabetes key enzymes, α-amylase and α-glucosidase

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