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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. [1] [2] The interaction between starch and the triiodide anion (I − 3) is the basis ...
Melzer's reagent is an aqueous solution of chloral hydrate, potassium iodide, and iodine.Depending on the formulation, it consists of approximately 2.50-3.75% potassium iodide and 0.75–1.25% iodine, with the remainder of the solution being 50% water and 50% chloral hydrate.
The iodometric titration is a general method to determine the concentration of an oxidising agent in solution. In an iodometric titration, a starch solution is used as an indicator since it can absorb the I 2 that is released, visually indicating a positive iodine-starch test with a deep blue hue. This absorption will cause the solution to ...
The Ripper Method, developed in 1898, [1] is an analytical chemistry technique used to determine the total amount of sulfur dioxide (SO 2) in a solution.This technique uses iodine standard and a starch indicator to titrate the solution and determine the concentration of free SO 2.
A redox titration [1] is a type of titration based on a redox reaction between the analyte and titrant. It may involve the use of a redox indicator and/or a potentiometer. A common example of a redox titration is the treatment of a solution of iodine with a reducing agent to produce iodide using a starch indicator to help detect the endpoint.
Sodium thiosulfate is used to reduce iodine back to iodide before the iodine can complex with the starch to form the characteristic blue-black color. Iodine is generated: 2 I − + S 2 O 2− 8 → I 2 + 2 SO 2− 4. And is then removed: I 2 + 2 S 2 O 2− 3 → 2 I − + S 4 O 2− 6. Once all the thiosulfate is consumed the iodine may form a ...
SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.
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