Abstract
Enzymes are commonly defined as biological catalysts, regulating particular biochemical reactions. α-Amylase (EC 3.2.1.1) is one of the industrially important enzymes, which are extensively used in starch hydrolyzing processes, such as brewing, fermentation, detergent production, food processing, etc. This enzyme breaks down α-1,4 glycosidic bonds in amylose or amylopectin. The end products from amylose are maltotriose and maltose. Maltose, glucose, and limit dextrin are formed from amylopectin. There are many studies in the literature regarding the α-amylase inhibitors, which have the potentials of being used in diabetes and obesity. However, there is a very limited number of studies in the literature about the activation of this enzyme, which could be harmful to such diseases. This study aims to support the activation activity of phloridzin, naringenin, and cinnamic acid for α-amylase, which was previously proved experimentally, with some in silico tests.
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