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The chart shows the level of residual starch. The cut surface of an apple stained with iodine, indicating a starch level of 4–5. The iodine–starch test is a chemical reaction that is used to test for the presence of starch or for iodine. The combination of starch and iodine is intensely blue-black.
The occurrence of starch degradation into sugar by the enzyme amylase was most commonly known to take place in the Chloroplast, but that has been proven wrong. One example is the spinach plant, in which the chloroplast contains both alpha and beta amylase (They are different versions of amylase involved in the breakdown of starch and they ...
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
Created Date: 8/30/2012 4:52:52 PM
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 ...
To generate energy, the plant hydrolyzes the starch, releasing the glucose subunits. Humans and other animals that eat plant foods also use amylase, an enzyme that assists in breaking down amylopectin, to initiate the hydrolysis of starch. [3] Starch is made of about 70–80% amylopectin by weight, though it varies depending on the source.
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.
A common protocol used in the past for zymography of α-amylase activity was the so-called starch film protocol of W.W. Doane. Here a native PAGE gel was run to separate the proteins in a homogenate. Subsequently, a thin gel with starch dissolved (or more properly, suspended) in it was overlaid for a period of time on top of the original gel. [6]