| Product Name | α-Amylase (AMS) Assay Reagent (Starch-iodine Colorimetric Method） |
| Catalog No. | ETR-HMM-0034 |
| Description | Amylase is present in animals (saliva, pancreas, etc.), plants (malt, horseradish), and microorganisms. Enzymes in microorganisms are almost exclusively secretory. This enzyme requires Ca²⁺ as an essential factor, which also acts as a stabilizing and activating factor. However, some amylases are non-Ca²⁺-dependent. Amylase acts on both linear starch and branched starch, randomly cleaving the α-1,4 bonds within the sugar chains without discrimination. Therefore, its characteristic is a sharp decrease in the viscosity of the substrate solution and the disappearance of the iodine reaction. The main end product in the hydrolysis of linear starch is glucose, Additionally, there are small amounts of maltotriose and maltose. Among these, fungal α-amylase primarily produces maltose as the final product of starch hydrolysis and does not contain high-molecular-weight limit dextrins, making it widely used in the baking industry and maltose manufacturing. On the other hand, when decomposing branched-chain starch, in addition to maltose, glucose, and maltotriose, α-limiting dextrin (also known as α-dextrin) with α-1,6 bonds in the branched portion is also produced. The general decomposition limit, measured by glucose, is 35–50%, but in bacterial amylase, there are also cases where the decomposition limit reaches as high as 70% (with glucose being the final free product). |
| Application | This product uses the starch-iodine colorimetric method to determine AMS activity. |
| Number of Testable Samples | 96 Samples |
| Detection Method | Starch-iodine colorimetric method |
For research use only, not for clinical use.
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