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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]
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 official analysis methods for the determination of diastase activity in honey are the Schade assay and Phadebas assays, recommended by the International Honey Commission. [14] As this method is based on fixed equations instead of a standard curve the new Phadebas honey diastase test was developed, to ensure stable results independent of batch.
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 glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas .
Glucan 1,4-alpha-maltohydrolase (EC 3.2.1.133, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with systematic name 4-alpha-D-glucan alpha-maltohydrolase. [ 1 ] [ 2 ] This enzyme catalyses the following chemical reaction
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
Beta-amylase [8] [9] is an enzyme that hydrolyzes 1,4-alpha-glucosidic linkages in starch-type polysaccharide substrates so as to remove successive maltose units from the non-reducing ends of the chains. Beta-amylase is present in certain bacteria as well as in plants. Three highly conserved sequence regions are found in all known beta-amylases.
The two enzymes have similar folding patterns and protein domains. In fact, past attempts to produce drugs targeting glucansucrase have not been successful because the drugs also disrupted amylase, which is necessary to break down starches. [12] [13] This occurred because the active sites of the two enzymes are nearly the same. Glucansucrase ...