Recent trends in production and potential applications of microbial amylases: A comprehensive review

Abstract

α-amylases are vital biocatalysts that constitute a billion-dollar industry with a substantial and enduring global demand. Amylases hydrolyze the α-1,4-glycosidic linkages in starch polymers to generate maltose and malto-oligosaccharides subunits. Amylases are key enzymes that have promising applications in various industrial processes ranging from pharmaceutical, pulp and paper, textile food industries to bioremediation and biofuel sectors. Microbial enzymes have been widely used in industrial applications owing to their ease of availability, cost-effectiveness and better stability at extreme temperatures and pH. α-amylases derived from distinct microbial origins exhibit diverse characteristics, which make them suitable for specific applications. The routine application of immobilized enzymes has become a standard practice in the production of numerous industrial products across the pharmaceutical, chemical, and food industries. This review details the structural makeup of microbial α-amylase to understand its thermodynamic characteristics, aiming to identify key areas that could be targeted for improving the thermostability, pH tolerance and catalytic activity of α-amylase through various immobilization techniques or specific enzyme engineering methods. Additionally, the review briefly explores the enzyme production strategies, potential sources of α-amylases, and use of cost-effective and sustainable raw materials for enzyme production to obtain α-amylases with unconventional applications in various industrial sectors. Major hurdles, challenges and future prospects involving microbial α-amylases has been briefly discussed by considering its diverse applications in industrial bioprocessing.

Keywords: Immobilizations; Industrial applications; Industrial enzymes; α-amylases.