α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in humans and other mammals.It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. [1]
Introduction
The (EC 3.2.1.1 ) (CAS# 9014-71-5) (alternative names: 1,4-α-D-glucan glucanohydrolase; glycogenase) are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. In animals, it is a major digestive enzyme, and its optimum pH is 6.7–7.0
In human physiology, both the salivary and pancreatic amylases are α-amylases.
The α-amylases form is also found in plants, fungi (ascomycetes and basidiomycetes) and bacteria (Bacillus) [2]
Industrial use
α-Amylase is used in ethanol production to break starches in grains into fermentable sugars.
The first step in the production of high-fructose corn syrup is the treatment of cornstarch with α-amylase, producing shorter chains of sugars oligosaccharides.
An α-amylase called "Termamyl", sourced from Bacillus licheniformis, is also used in some detergents, especially dishwashing and starch-removing detergents.[3]
Relevance
Structural highlights
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