Enzyme Engineering
Open Access

Amylase: Types and Applications

Alyssa Conanain^{* *}Correspondence: Dr. Alyssa Conanain, Department of Biotechnology, North Carolina State University, Raleigh, USA, Email:

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Description

Amylase is an enzyme observed in the saliva of human beings and a few different mammals. The breakdown of starch into sugars is catalysed by salivary amylase, also known as ptyalin. Salivary -amylases, vertebrate pancreas, and the bacterial -amylase from Alteromonas haloplanctis all have chloride as an allosteric effector. A few monovalent anions were utilised to undertake activation tests on Alteromonas haloplanctis, which revealed that the amylolytic reaction requires a low charge. Additionally, the structures of the chloride binding site reveal that a basic residue is an important component of the site. The binding affinity of Cl^– is impacted by the chloride coordination mechanism used by that basic residue, according to a comparison of the kd values for Cl^– in three homologous -amylases. According to the allosteric kinetic model, a thorough examination of chloride binding and substrate reveals that the chloride effector has no function in substrate binding. But, the experiments of chemical modifications, pH dependence of action, and calcium ions inhibitions determine that chloride ions are liable for the pKa shift of the catalytic groups and interface with active site carboxyl groups. Amylase is a member of a family of enzymes that catalyse the hydrolysis (breaking of a substance by the addition of a water molecule) of starch into minor carbohydrate units like maltose, which includes two glucose molecules. The three classes of amylases, denoted with letters alpha, beta, and gamma, differ in how they attack the starch molecules' bonds. Alpha-amylase is common among living organisms. In the digestive systems of humans and many other mammals, an alpha-amylase which is also known as ptyalin is made by the salivary glands, whereas pancreatic amylase is produced by the pancreas into the small intestine. The optimal pH of alpha-amylase is 6.7–7.0. Ptyalin is assosiated with food in the mouth, which acts upon starches. Though the food residues remain in the mouth for a short time, the activity of ptyalin lasts for up to several hours in the stomach —till the food is mixed with the stomach secretions, high acidity may leads to inactivation of ptyalin. Ptyalin’s digestive action based upon how far acid is in the stomach, how promptly the stomach contents empty, and how exhaustively the food has mixed with the acid. Under optimum environments 35 to 50 percent of ingested starches can be break down to maltose by action of ptyalin during ingestion in the stomach. When food permits to the small intestine, the rest of the starch molecules are catalysed mostly to maltose by pancreatic amylase. This is the first step in starch digestion occurs in the small intestine (the duodenum), the region into which the pancreatic juices get empty. For the conversion of starches to oligosaccharides, the enzyme -amylase is necessary. Starch is a significant constituent of the human diet and is a chief storage product of various economically important crops such as Rice, wheat, tapioca, maize, and potato. Starch-converting enzymes are mainly used in the production of, modified starches, maltodextrin, or fructose and glucose syrups. There are huge number of microbial α- amylases have been using in different industrial sectors such as textile, food, detergent and paper industries. The production of α-amylases has usually been done using submerged fermentation, however solid state fermentation systems seem as a favourable technology. The pH profile, thermostability, pH stability, and Ca-independency of each -amylase are important in the growth of the fermentation process.