amülaase

Amülaase is an enzyme that catalyzes the hydrolysis of starch and related carbohydrates into smaller sugars, such as maltose and glucose. It belongs to the carbohydrase family and is essential for the digestion of starch in many animals as well as for various plant and microbial processes.

Several forms exist. α-amülaase is endo-acting and splits internal α-1,4 glycosidic linkages; in humans it is produced by the salivary glands and the pancreas. β-amülaase is found mainly in plants and some microbes, while γ-amülaase (glucoamylase) cleaves both α-1,4 and α-1,6 bonds to release glucose.

Biochemical properties include dependence on calcium ions for stability and an optimum pH near neutral, with activity varying by source. α-amülaase typically functions best around pH 6–7 in the mouth and small intestine, while γ-amülaase often tolerates a broader pH range.

Biological roles encompass starch digestion in humans and animals, digestion of stored starch in germinating seeds, and other carbohydrate-processing tasks in plants and microbes. Industrially, amülaases are used to produce fermentable sugars in brewing and baking, convert starch to syrups, and serve in detergents and textile processing.

Clinically, serum amülaase measurement supports the diagnosis of pancreatitis and certain salivary gland disorders, though it is less specific than lipase in current practice. Normal levels do not exclude disease, and elevations warrant clinical correlation.