|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
- Hydrolysis of (1->4)-alpha-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
- 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. PMID 21085740.
- Balls AK, Walden MK, Thompson RR (March 1948). "A crystalline beta-amylase from sweet potatoes". The Journal of Biological Chemistry. 173 (1): 9–19. PMID 18902365.
- French D (1960). "β-Amylases". In Boyer PD, Lardy H, Myrbaumlck K. The Enzymes. 4 (2nd ed.). New York: Academic Press. pp. 345–368.
- Manners DJ (1962). "Enzymic synthesis and degradation of starch and glycogen". Advances in Carbohydrate Chemistry. 17: 371–430. doi:10.1016/s0096-5332(08)60139-3.
- "Amylase, Alpha" , I.U.B.: 220.127.116.11,4-α-D-Glucan glucanohydrolase.