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β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. [ 2 ] [ 3 ] [ 4 ] It catalyses the following reaction: Hydrolysis of (1→4)-α- D -glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
An amylase (/ ˈ æ m ɪ l eɪ s /) is an enzyme that catalyses the hydrolysis of starch (Latin amylum) into sugars. Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion .
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.
Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...
These enzymes have a variety of uses including degradation of plant materials (e.g., cellulases for degrading cellulose to glucose, which can be used for ethanol production), in the food industry (invertase for manufacture of invert sugar, amylase for production of maltodextrins), and in the paper and pulp industry (xylanases for removing ...
Alpha-glucosidases are enzymes involved in breaking down complex carbohydrates such as starch and glycogen into their monomers. [2] They catalyze the cleavage of individual glucosyl residues from various glycoconjugates including alpha- or beta-linked polymers of glucose. This enzyme convert complex sugars into simpler ones.
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