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
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[5] They belong to Glycoside hydrolase family 14.
See also
[edit]References
[edit]- ^ 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 β-amylase from sweet potatoes". The Journal of Biological Chemistry. 173 (1): 9–19. doi:10.1016/S0021-9258(18)35550-9. PMID 18902365.
- ^ French D (1960). "β-Amylases". In Boyer PD, Lardy H, Myrbaumlck K (eds.). The Enzymes. Vol. 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. ISBN 9780120072170.
- ^ "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase.
Further reading
[edit]- Friedberg F, Rhodes C (March 1986). "Cloning and characterization of the β-amylase gene from Bacillus polymyxa". Journal of Bacteriology. 165 (3): 819–24. doi:10.1128/JB.165.3.819-824.1986. PMC 214501. PMID 2419310.
- Rhodes C, Strasser J, Friedberg F (May 1987). "Sequence of an active fragment of B. polymyxa β amylase". Nucleic Acids Research. 15 (9): 3934. doi:10.1093/nar/15.9.3934. PMC 340808. PMID 2438660.
External links
[edit]- "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase. "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase.
External links
[edit]- Beta-amylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
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