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α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]
Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene. [3] This gene is found in many organisms. Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and g
The intake of a single dose of alpha-amylase inhibitor before a meal containing complex carbohydrates clearly suppresses the glucose spike and may decrease the postprandial hyperglycemia (higher than 140 mg/dL; >7.8 mmol/L) in patients with type II diabetes. [1]
Hydrolysis reaction of Maltose being broken at the 1-4 alpha-glucosidase linkage. The mechanism of all FamilyGH13 enzymes is to break a α-glucosidase linkage by hydrolyzing it. Maltase focuses on breaking apart maltose, a disaccharide that is a link between 2 units of glucose, at the α-(1->4) bond.
An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid. [10] When used as a food additive, amylase has E number E1100, and may be derived from pig pancreas or mold fungi. Bacilliary amylase is also used in clothing and dishwasher detergents to dissolve starches from fabrics and dishes.
Glucan 1,4-α-glucosidase (EC 3.2.1.3, glucoamylase, amyloglucosidase, γ-amylase, lysosomal α-glucosidase, acid maltase, exo-1,4-α-glucosidase, glucose amylase, γ-1,4-glucan glucohydrolase, acid maltase, 1,4-α-D-glucan glucohydrolase) is an enzyme located on the brush border of the small intestine with systematic name 4-α-D-glucan glucohydrolase.
Glucose levels vary before and after meals, and at various times of day; the definition of "normal" varies among medical professionals. In general, the normal range for most people (fasting adults) is about 4 to 6 mmol/L or 80 to 110 mg/dL. (where 4 mmol/L or 80 mg/dL is "optimal".)
In molecular biology, glycoside hydrolase family 13 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety.