Amylase

Amylase (amylase, AMY, AMS) generally act on soluble starch, amylose, glycogen and other α-1,4- glucan, α-1,4- glycosidic bond hydrolysis enzyme. According to the role can be divided into α- amylase (EC3.2.1.1.) And β- amylase (EC3.2.1.2.). (1) α- amylase is widely distributed in animals (saliva, pancreas, etc.), plants (malt, wasabi) and microorganisms. Almost all microbial enzyme secretory. This enzyme is essential to Ca2 + as a stabilizing factor and factors, both acting on amylose, amylopectin also applied, indiscriminately cutting α-1,4- chain. Accordingly, characterized in that the disappearance of a substrate solution causing a sharp drop in viscosity and iodine reaction, the final product in the decomposition of amylose to maltose based, in addition, there are small amounts of maltotriose and glucose. On the other hand in the decomposition of amylopectin, in addition to maltose, grape sugar α- amylase, but also generates the branch portion having α-1,6- linkages α- limit dextrin. General glucose decomposition limit, whichever is 35-50%, but in amylase bacteria, there are also presented decomposition limit of up to 70% (final free glucose); (2) β- amylase and α- amylase The difference is that from the non-reducing end successive maltose units off α-1,4- glucan chains. Mainly found in higher plants (barley, wheat, sweet potato, soybean, etc.), but also reported the presence of bacteria, milk, mold in. For as amylose as no branch can be completely decomposed substrate maltose and a small amount of glucose. Act on amylopectin or dextran, when cut to the front of the reaction α-1,6- bonds stopped, thus generating a relatively large molecular weight limit dextrin. From the above α- amylase and β- amylase mode of action, it is proposed -4- glucose α-1,4- glucan hydrolase (α-1,4-glucan 4-glucanohydrolase) and α-1, 4- glucan - maltose hydrolase (α-1,4-glucan maltohydrolase) name, etc. being used.