Structure-based modification of a-amylase by conventional and emerging technologies: Comparative study on the...

α-Amylase is an endo-enzyme that catalyzes the hydrolysis of starch into shorter oligosaccharides. α-Amylase plays a crucial role in various industries. Manipulated α-amylases are of particular interest due to their remarkable amylolysis efficiency and thermostability for large-scale biotechnological processes. The retained catalytic activity of enzymes is decreased according to extreme pH, temperature, pressure, and chemical reagents. Broad industrial applications of α-amylases need special properties such as stability against temperature, pH, and chelators, and also attain reusability, desirable enzymatic activity, efficiency, and selectivity. Considering the biotechnological importance of α-amylase, its high stability is the most critical challenge for its economic viability. Therefore, improving its functionality and stability recently gained much interest. To achieve this purpose, various emerging technologies in combination with conventional methods on α-Amylases with different sources have been conducted. The present review is an attempt to summarize the effect of various conventional methods and emerging technologies employed to date on α-amylase secondary structure, thermal stability, and performance.