2016
DOI: 10.1016/j.jep.2016.02.024
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Kinetics of α -amylase and α -glucosidase inhibitory potential of Zea mays Linnaeus (Poaceae), Stigma maydis aqueous extract: An in vitro assessment

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Cited by 82 publications
(50 citation statements)
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“…The IC 50 value for αglucosidases inhibition with acarbose was 126 μg/ml. This IC 50 value fell within the range of IC 50 values (35.5-500 μg/ml) reported by other authors for acarbose (Loizzo et al, 2015;Sabiu, O'Neill, & Ashafa, 2016).…”
Section: Inhibition Of Intestinal Rat α-Glucosidasessupporting
confidence: 89%
“…The IC 50 value for αglucosidases inhibition with acarbose was 126 μg/ml. This IC 50 value fell within the range of IC 50 values (35.5-500 μg/ml) reported by other authors for acarbose (Loizzo et al, 2015;Sabiu, O'Neill, & Ashafa, 2016).…”
Section: Inhibition Of Intestinal Rat α-Glucosidasessupporting
confidence: 89%
“…Early work has shown that corn silk and corn bran contain polysaccharides, and their antioxidant and anticoagulant activities of polysaccharides have been reported (Hu and others ). The hypoglycemic mechanism of stigma polysaccharide shows that the corn silk polysaccharides are inhibitors of α‐amylase and α‐glucosidase which together offer an effective strategy to modulate levels of post‐prandial hyperglycaemia via control of starch metabolism (Sabiu and others ). The expression levels of TGF‐β1 diabetic rat kidneys and triglyceride level are reduced significantly in corn silk, which restrains macrophages to protect the kidneys of diabetic rats (Wen and others ).…”
Section: Resultsmentioning
confidence: 99%
“…As presented in this study, CEE had significant inhibitory effect on the specific activities of -amylase and -glucosidase. Judging by the IC50 values and relative to the standard, it was evident that the extract elicited a stronger inhibition on the activity ofglucosidase than -amylase and this is therapeutically significant in abolishing the adverse effects consistent with the conventional -glucosidase and -amylase inhibitors (Sabiu et al, 2016b). The competitively inhibited activity of the α-amylase is indicative of a stronger structural resemblance of the major constituent of the extract to the substrate which facilitated its favourable binding on the active site of the enzyme at the expense of the substrate.…”
Section: Discussionmentioning
confidence: 99%
“…This was achieved following reported methods (Elsnoussi et al, 2012;Sabiu et al, 2016b). Briefly, known concentrations (0.25-10.0 mg/mL) of the extract or acarbose (standard) were prepared and 500 µL of each was mixed with 500 µL of 0.02 M sodium phosphate buffer (pH 6.9) containing 0.5 mg/mL of ice cold porcine pancreatic α-amylase solution in test tubes.…”
Section: In Vitro Antidiabetic Assays Kinetics Of α-Amylase Inhibitionmentioning
confidence: 99%