Amylase: Difference between revisions
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<StructureSection load='1hvx' size='400' side='right' scene='Sandbox_182/Alpha-amylase/1' caption=''> | |||
=Introduction= | =Introduction= | ||
Discovered and isolated by [http://en.wikipedia.org/wiki/Anselme_Payen Anselme Payen] in 1833, amylase was the first enzyme to be discovered<ref name="book">Yamamoto T.1988. Handbook of Amylases and Related Enzymes: Their Sources, Isolation Methods, Properties and Applications. Osaka Japan: Pergamon Press</ref>. Amylases are hydrolases, acting on α-1,4-glycosidic bonds<ref name="Path">PMID:9541387</ref>. They can be further subdivided into α,β and γ amylases<ref name="book"/>.'''α-Amylase''' (AAM) is an enzyme that acts as a catalyst for the hydrolysis of alpha-linked polysaccharides into α-anomeric products<ref name="Main">PMID:11226887</ref>. The enzyme can be derived from a variety of sources, each with different characteristics. α-Amylase found within the human body serves as the enzyme active in pancreatic juice and salvia<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries. Beta/alpha amylase (BAAM) is a precursor protein which is cleaved to form the beta-amylase and alpha-amylase after secretion. | Discovered and isolated by [http://en.wikipedia.org/wiki/Anselme_Payen Anselme Payen] in 1833, amylase was the first enzyme to be discovered<ref name="book">Yamamoto T.1988. Handbook of Amylases and Related Enzymes: Their Sources, Isolation Methods, Properties and Applications. Osaka Japan: Pergamon Press</ref>. Amylases are hydrolases, acting on α-1,4-glycosidic bonds<ref name="Path">PMID:9541387</ref>. They can be further subdivided into α,β and γ amylases<ref name="book"/>.'''α-Amylase''' (AAM) is an enzyme that acts as a catalyst for the hydrolysis of alpha-linked polysaccharides into α-anomeric products<ref name="Main">PMID:11226887</ref>. The enzyme can be derived from a variety of sources, each with different characteristics. α-Amylase found within the human body serves as the enzyme active in pancreatic juice and salvia<ref name="Path"/>. α-Amylase is not only essential in human physiology but has a number of important biotechnological functions in various processing industries. Beta/alpha amylase (BAAM) is a precursor protein which is cleaved to form the beta-amylase and alpha-amylase after secretion. | ||
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α-Amylase is used extensively in various industrial processes. In textile weaving, starch is added for warping. After weaving, the starch is removed by ''Bacillus subtilis'' α-amylase<ref name="book"/>. Dextrin, which is a viscosity improver, filler, or ingredient of food, is manufactured by the liquefaction of starch by bacteria α-amylase<ref name="book"/>. Bacterial α-amylases of ''B.subtilis'', or ''B.licheniformis'' are used for the initial starch liquefaction in producing high conversion glucose syrup<ref name="book"/>. Pancreatitis can be tested by determining the level of amylases in the blood, a result of damaged amylase-producing cells, or excretion due to renal failure<ref>PMID: 16286272 </ref>. α-Amylase is used for the production of malt, as the enzyme is produced during the germination of cereal grains<ref name="book"/>. | α-Amylase is used extensively in various industrial processes. In textile weaving, starch is added for warping. After weaving, the starch is removed by ''Bacillus subtilis'' α-amylase<ref name="book"/>. Dextrin, which is a viscosity improver, filler, or ingredient of food, is manufactured by the liquefaction of starch by bacteria α-amylase<ref name="book"/>. Bacterial α-amylases of ''B.subtilis'', or ''B.licheniformis'' are used for the initial starch liquefaction in producing high conversion glucose syrup<ref name="book"/>. Pancreatitis can be tested by determining the level of amylases in the blood, a result of damaged amylase-producing cells, or excretion due to renal failure<ref>PMID: 16286272 </ref>. α-Amylase is used for the production of malt, as the enzyme is produced during the germination of cereal grains<ref name="book"/>. | ||
β/α amylase (BAAM) is a precursor protein which is cleaved to form the β-amylase and α-amylase after secretion. | β/α amylase (BAAM) is a precursor protein which is cleaved to form the β-amylase and α-amylase after secretion. | ||
</StructureSection> | |||
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=3D structures of Amylase= | =3D structures of Amylase= | ||