Amilasas

Amilasas, or amylases, are enzymes that catalyze the hydrolysis of starch and related polysaccharides into smaller carbohydrate units. They are found across many living organisms, including humans, plants, and microorganisms, and play essential roles in digestion as well as in various industrial processes.

In humans, the two principal forms are salivary amylase (ptyalin) and pancreatic amylase. Salivary amylase is produced by the salivary glands and initiates starch digestion in the mouth, while pancreatic amylase is secreted by the pancreas into the small intestine to continue digestion. Both forms act best near neutral pH and require ions such as calcium for stability; chloride ions specifically enhance the activity of pancreatic amylase.

Biochemically, amilasas primarily cleave alpha-1,4 glycosidic bonds in starch, producing maltose, maltotriose, and dextrins. They do not efficiently hydrolyze alpha-1,6 bonds at branch points; debranching enzymes are required for complete starch breakdown to glucose. Amilasas belong to the glycoside hydrolase family 13, and their activity is influenced by pH, temperature, and ion availability.

Clinical and industrial relevance is broad. Clinically, measuring serum amylase can aid in assessing pancreatic function and diagnosing certain conditions, though it is often supplemented by lipase testing. In industry, amilasas are widely used in baking, brewing, and starch processing, as well as in detergents for stain removal, due to their starch-degrading capabilities. The term amilasa/amilasas reflects Spanish- and other Romance-language usage, while the English term is amylase.

The discovery of amylase dates to 1833, when Anselme Payen and Jean Persoz identified the enzyme and named it diastase, later recognized as amylase in broader contexts.