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Many bacteria like Bacillus subtilis can produce such an enzyme to help scientists identify unknown bacterial samples -- the starch-iodine test is one of many tests needed to identify the exact bacterium. [13] The positive test for bacteria that has starch hydrolysis capabilities (able to produce amylase) is the presence of a yellow zone around ...
The starch iodine test, a development of the iodine test, is based on colour change, as α-amylase degrades starch and is commonly used in many applications. A similar but industrially produced test is the Phadebas amylase test, which is used as a qualitative and quantitative test within many industries, such as detergents, various flour, grain ...
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
An amylase (/ ˈ æ m ɪ l eɪ s /) is an enzyme that catalyses the hydrolysis of starch (Latin amylum) into sugars. Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion .
A diastase (/ ˈ d aɪ ə s t eɪ z /; from Greek διάστασις, "separation") is any one of a group of enzymes that catalyses the breakdown of starch into maltose.For example, the diastase α-Amylase degrades starch to a mixture of the disaccharide maltose; the trisaccharide maltotriose, which contains three α (1-4)-linked glucose residues; and oligosaccharides, known as dextrins, that ...
Amylase breaks down carbohydrates into mono- and disaccharides, so a starch agar must be used for this assay. Once the bacteria is streaked on the agar, the plate is flooded with iodine. Since iodine binds to starch but not its digested by-products, a clear area will appear where the amylase reaction has occurred.
β-amylase catalyses the hydrolysis of starch into maltose by the process of removing successive maltose units from the non-reducing ends of the chains. γ-Amylase will cleave the last α(1–4)glycosidic linkages at the nonreducing end of amylose and amylopectin, yielding glucose.
Klebsiella aerogenes, [2] previously known as Enterobacter aerogenes, is a Gram-negative, oxidase-negative, catalase-positive, citrate-positive, indole-negative, rod-shaped bacterium. [3] Capable of motility via peritrichous flagella, [ 4 ] it is approximately one to three microns in length.