B - amylase - wikipedia B - amylase Beta - amylase Structure of barley beta - amylase. PDB 2xfr Identifiers EC number 3.2. 1.2 CAS number 9000 - 91 - 3 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Gene Ontology AmiGO / QuickGO Search PMC articles PubMed articles NCBI proteins Beta - amylase ( EC 3.2. 1.2, saccharogen amylase, glycogenase ) is an enzyme with the systematic name 4 - alpha - D - glucan maltohydrolase. This enzyme catalyses the following chemical reaction 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 See also Amylase Alpha - amylase References Jump up ^ Rejzek, M. ; Stevenson, C.E. ; Southard, A.M. ; Stanley, D. ; Denyer, K. ; Smith, A.M. ; Naldrett, M.J. ; Lawson, D.M. ; Field, R.A. ( 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 -- 730. PMID 21085740. doi : 10.1039 / c0mb00204f. Jump up ^ Balls, A.K. ; Walden, M.K. ; Thompson, R.R. ( 1948 ). `` A crystalline β - amylase from sweet potatoes ''. J. Biol. Chem. 173 : 9 -- 19. Jump up ^ French, D. ( 1960 ). `` β - Amylases ''. In Boyer, P.D. ; Lardy, H. ; Myrbaumlck, K. The Enzymes. 4 ( 2nd ed. ). New York : Academic Press. pp. 345 -- 368. Jump up ^ Manners, D.J. ( 1962 ). `` Enzymic synthesis and degradation of starch and glycogen ''. Adv. Carbohydr. Chem. 17 : 371 -- 430. doi : 10.1016 / s0096 - 5332 ( 08 ) 60139 - 3. Jump up ^ `` Amylase, Alpha '', I.U.B. : 3.2. 1.11, 4 - α - D - Glucan glucanohydrolase. External links Beta - amylase at the US National Library of Medicine Medical Subject Headings ( MeSH ) Hydrolase : sugar hydrolases ( EC 3.2 ) 3.2. 1 : Glycoside hydrolases Disaccharidase Sucrase / Sucrase - isomaltase / Invertase Maltase Trehalase Lactase Glucosidases Cellulase Alpha - glucosidase Acid Neutral AB Neutral C Beta - glucosidase cytosolic Debranching enzyme Other Amylase Alpha - amylase Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases Alpha Beta alpha - Mannosidase Glucuronidase Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase Alpha - N - acetylgalactosaminidase NAGA Alpha - N - acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase - glucoamylase Heparanase HPSE2 3.2. 2 : Hydrolysing N - Glycosyl compounds DNA glycosylases : Oxoguanine glycosylase Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie -- Hofstee diagram Hanes -- Woolf plot Lineweaver -- Burk plot Michaelis -- Menten kinetics Types EC1 Oxidoreductases ( list ) EC2 Transferases ( list ) EC3 Hydrolases ( list ) EC4 Lyases ( list ) EC5 Isomerases ( list ) EC6 Ligases ( list ) Molecular and Cellular Biology portal Retrieved from `` https://en.wikipedia.org/w/index.php?title=B-amylase&oldid=776330437 '' Categories : EC 3.2. 1 Talk Search About Wikipedia 日本 語 Српски / srpski Srpskohrvatski / српскохрватски Edit links This page was last edited on 20 April 2017, at 10 : 11. Text is available under the Creative Commons Attribution - ShareAlike License ; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia ® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization. About Wikipedia

Question: what kinds of bonds are broken by b-amylase
Answer: glycosidic bond