Amylases are essential biological catalysts that hydrolyze glycosidic bonds in starch, generating sugars such as maltose, maltotriose, and dextrin, with alpha-amylase from the GH13 family being especially significant due to its efficient polysaccharide-degrading ability. Its activity depends on conserved catalytic residues located within an (α/β)₈-barrel domain, supported by calcium ions that enhance enzyme stability. Microbial amylases, particularly from bacterial and fungal sources, account for nearly 25% of the industrial enzyme market because of their high productivity, robustness, and cost-effective cultivation. Their production is regulated by key physicochemical factors including pH, temperature, nutrient sources, and fermentation conditions, with solid-state or submerged fermentation. Recent advances in biotechnology have accelerated efforts to enhance amylase properties through recombinant DNA technology, site-directed mutagenesis, and screening of extremophilic strains for natural thermostability. These approaches have successfully improved catalytic efficiency, thermostability, and overall industrial performance. Integrating microbial diversity exploration with molecular engineering and optimized fermentation processes continues to drive the development of next-generation amylases tailored for diverse applications.