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glucosidase

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glucosidase /glu·co·si·dase/ (gloo-ko´sĭ-dās) any of a group of enzymes of the hydrolase class that hydrolyze glucose residues from glucosides; they are specific for α- or β- configurations as well as for particular substrate configurations, e.g., maltase.
glu·co·si·dase (gl-ks-ds, -dz)
n.
Any of various enzymes that catalyze glucoside hydrolysis.

glucosidase [gloo-ko´sĭ-dās]
an enzyme of the hydrolase class that splits glucoside, occurring as α-, β-, and α-1,3-glucosidase; α-glucosidase (maltase) occurs in intestinal juice, and β-glucosidase (cellobiase) in the kidney, liver, and intestinal mucosa.

glucosidase
an enzyme of the hydrolase class that cleaves the glucosidic bond between two glucose molecules, occurring as α-, β- and α-1,3-glucosidase; α-glucosidase (maltase) occurs in intestinal juice, and β-glucosidase (cellobiase) in the kidney, liver and intestinal mucosa.


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It works to block both alpha amylase and alpha glucosidase enzymes; reduces peak glucose levels by 90% and peak insulin levels by 40% 30 minutes after consuming a high starch meal; and eliminates the period of hypoglycemia that is common after a high glycemic index meal.
Kalidas Shetty and colleagues from the University of Massachusetts (USA) have found that red wine inhibits the activity of alpha glucosidase, an enzyme responsible for triggering the absorption of glucose by the small intestine, by almost 100%; black tea extracts produce a 90% inhibitory effect.
Classifications include: biguanides; glucosidase inhibitors; meglitinides; sulphonylureas; dipeptidyl peptidase-4 inhibitor; and thiazolidinediones (1).
 
 
 
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