amilases

Amylases are enzymes that catalyze the hydrolysis of starch and related carbohydrates, converting them into smaller sugars such as maltose and glucose. They belong to the glycoside hydrolase family and function optimally in aqueous environments.

The main types are alpha-amylase, beta-amylase, and glucoamylase. Alpha-amylase is an endo-acting enzyme that cleaves internal alpha-1,4-glycosidic bonds in starch, producing dextrins and smaller sugars. Beta-amylase is exo-acting and releases maltose from the non-reducing ends. Glucoamylase (also called amyloglucosidase) cleaves both alpha-1,4- and alpha-1,6-linkages to yield glucose. These enzymes are found in diverse organisms: human and animal saliva and pancreas contain alpha-amylase; plants and microbes produce beta-amylases; fungi and bacteria commonly produce glucoamylases.

Properties: Many amylases require calcium ions for structural stability; some mammalian amylases are activated by chloride. pH and temperature optima vary by source, with industrial variants often active around pH 4.5–7 and temperatures up to 50–80 C. They act on starch, amylose, amylopectin, and related polysaccharides.

Applications: Amylases are used to convert starch to sugars in food and beverage production, including baking, brewing, and syrup production. They are added to detergents to remove starchy soils and to textile processing. In biotechnology, amylases are used to liquefy starch in saccharification steps of bioethanol production.

Medical relevance: Clinically, serum amylase measurements aid in diagnosing pancreatic or salivary gland disorders; elevated levels can indicate pancreatitis or salivary gland inflammation, while low levels may reflect exocrine pancreatic insufficiency or certain genetic conditions.