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(Redirected from Beta-Amylase)
Enzyme that hydrolyses alpha-1,4-D-glucosidic bonds in polysaccharides
β-Amylase (EC3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name4-α-D-glucan maltohydrolase. 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
This enzyme acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. Beta-amylase is found in bacteria, fungi, and plants; bacteria and cereal sources are the most heat stable. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit.
β-amylase is present in an inactive form prior to seed germination. Many microbes also produce amylase to degrade extracellular starches. Animal tissues do not contain β-amylase, although it may be present in microorganisms contained within the digestive tract. The optimum pH for β-amylase is 4.0–5.0 They belong to Glycoside hydrolase family 14.
Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA (March 2011). "Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase". Molecular BioSystems. 7 (3): 718–30. doi:10.1039/c0mb00204f. PMID21085740.
Structure of barley beta-amylase. PDB 2xfr