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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 ...
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 ...
Pancreatic alpha-amylase 1HNY. Amylases are a group of extracellular enzymes (glycoside hydrolases) that catalyze the hydrolysis of starch into maltose. These enzymes are grouped into three classes based on their amino acid sequences, mechanism of reaction, method of catalysis and their structure. [16]
Created Date: 8/30/2012 4:52:52 PM
Another form of amylase, β-amylase (EC 3.2.1.2 ) (alternative names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase) is also synthesized by bacteria, fungi, and plants. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units at a
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.
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
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]