Products
Amylases are available, for example, in the form of capsules together with other digestive enzymes. They are often present in industrially produced bread and pastries. The enzymes‘ name is derived from (starch), which is their substrate.
Structure and properties
Amylases are natural enzymes that hydrolytically cleave glycosidic bonds. They belong to the class of hydrolases. They are found in humans, animals, plants (e.g., in cereals), and microorganisms. For industrial use, they are usually obtained from fungi such as or from bacteria. Amylases, together with other digestive enzymes, are contained in pancreatin (pancreatic powder), which is obtained from the fresh or frozen pancreas of mammals, e.g. from pigs or cattle. Humans produce amylases in the salivary glands and in the pancreas. Thus, they are active in the mouth and small intestine.
Effects
The α-amylases cleave the α-1,4-glycosidic bond at random sites in starch and glycogen. This results in dextrins, larger oligosaccharides, the trisaccharide maltotriose, and the disaccharide maltose. The β-amylases also hydrolyze the α-1,4-glycosidic bond. They do not cut randomly, but detach the disaccharide maltose (glucose-glucose). γ-Amylases cleave single glucose molecules. Amylases are used in bread making because they break down starch into smaller carbohydrates, which serve as substrates for yeast. The yeast forms carbon dioxide and ethanol from the sugars. This causes the dough to rise. Amylases are involved in the ripening process of fruits, giving them a sweet taste.
Applications
Medicinal products:
- As a component of pancreatin, amylases are approved for the treatment of digestive disorders, for example, with bloating and flatulence, and in hypofunction of the pancreas.
Food:
