Bacterial Alpha Amylase

Amylase is a digestive enzyme classified as a saccharidase (an enzyme that cleaves polysaccharides). It is mainly a constituent of pancreatic juice and saliva, needed for the breakdown of long-chain carbohydrates (such as starch) into smaller units.

Amylase is a digestive enzyme made primarily by the pancreas and salivary glands. Enzymes are substances made and used by the body to trigger specific chemical reactions. The primary function of the enzyme amylase is to break down starches in food so that they can be used by the body. Amylase is also synthesised in the fruit of plants during ripening, causing them to become sweeter.

Amylases are enzymes that catalyze the hydrolysis of alpha-1, 4 glycosidic linkages of polysaccharides to yield dextrins, oligosaccharides, maltose and D-glucose. Amylases are derived from animal, fungal and plant sources. Pancreatin and pancrelipase contain amylase derived from the pancreas of animals, usually porcine pancreas.

Amylase is also derived from barley malt and the fungus Aspergillus oryzae. There are a few different amylases. These enzymes are classified according to the manner in which the glysosidic bond is attacked. Alpha-amylases hydrolyze alpha-1, 4-glycosidic linkages, randomly yielding dextrins, oligosaccharides and monosaccharides. Alpha-amylases are endo- amylases. Exoamylases hydrolyze the alpha-1, 4-glycosidic linkage only from the non-reducing outer polysaccharide chain ends. Exoamylases include beta-amylases and glucoamylases (gamma-amylases, amyloglucosidases). Beta-amylases yield beta-limit dextrins and maltose. Gamma-amylases yield glucose. Amylases are used as digestants.

Amylase is a calcium dependent enzyme which hydrolyzes complex carbohydrates at alpha 1,4-linkages to form maltose and glucose. a-Amylase catalyzes the hydrolysis of internal (endoglycosidase) a-1,4-glucan links in polysaccharides containing 3 or more a-1,4-linked D-glucose units (amylose and amylopectin) yielding a mixture of maltose and glucose..

Alpha-Amylase (1,4-a-D-glucan glucanohydrolase) in animals are monomeric, calcium-binding proteins that are present in both salivary and pancreatic secretions. In the gastrointestinal tract, it is a digestive enzyme that is secreted into the Duodenum where it starts to degrade (hydrolyze) the a-1,4 glucosidic linkages of starch to maltose and maltotriose. a-Amylases are used to hydrolyze glycogen, the reserve carbohydrates in animals, when the blood glucose levels are low. Salivary amylase, a major component of human salivary secretions, possesses multiple functions in the oral cavity. It is the only enzyme in the saliva capable of degrading oligosaccharides, which are used by the oral microflora for nutritional purposes.

Bacterial Alpha Amylase is obtained from Bacilus subtilis. Being an endoamylase it randomly hydrolyses alpha (1,4) glucosidic linkages of amylose and amylopectin of gelatinized starch to produce dextrins of various chain lengths and oligo saccharides. Glucose and maltose are also produced depending on the degree of hydrolysis. Because of this starch degrading ability of Bacterial Alpha Amylase, it is widely used in pharmaceutical industry in various digestive aid preparations. Due to presence of Bacterial Alpha Amylase, starch in the consumed food is better digested and this increases overall digestibility of food. Such digestive aid preparations are used for treatment of patient whose digestive power is reduced due to illness. Many such commercial formulations of digestive aids are seen in drug stores either as syrup or as tablet.