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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
Enzymes containing this domain belong to family 13 of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose .
The speed at which the stirrer falls is determined by the viscosity of the slurry. Samples with more sprouted grain have greater alpha-amylase activity, which will result in a less viscous slurry and a smaller falling number. Samples with less alpha-amylase activity will be more viscous and have a larger falling number.
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.
A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases. [3] The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme.
The % purity is 100% × (specific activity of enzyme sample / specific activity of pure enzyme). The impure sample has lower specific activity because some of the mass is not actually enzyme. If the specific activity of 100% pure enzyme is known, then an impure sample will have a lower specific activity, allowing purity to be calculated and ...
Isoamylase (EC 3.2.1.68, debranching enzyme, glycogen α-1,6-glucanohydrolase) is an enzyme with systematic name glycogen 6-α-D-glucanohydrolase. [1] It catalyses the hydrolysis of (1→6)-α-D-glucosidic branch linkages in glycogen, amylopectin and their β-limit dextrins. It also readily hydrolyses amylopectin.