Structural and functional adaptation in extremophilic microbial α-amylases

Abstract

Maintaining stable native conformation of a protein under a given ecological condition is the prerequisite for survival of organisms. Extremophilic bacteria and archaea have evolved to adapt under extreme conditions of temperature, pH, salt, and pressure. Molecular adaptations of proteins under these conditions are essential for their survival. These organisms have the capability to maintain stable, native conformations of proteins under extreme conditions. The enzymes produced by the extremophiles are also known as extremozyme, which are used in several industries. Stability and functionality of extremozymes under varying temperature, pH, and solvent conditions are the most desirable requirement of industry. α-Amylase is one of the most important enzymes used in food, pharmaceutical, textile, and detergent industries. This enzyme is produced by diverse microorganisms including various extremophiles. Therefore, understanding its stability is important from fundamental as well as an applied point of view. Each class of extremophiles has a distinctive set of dominant non-covalent interactions which are important for their stability. Static information obtained by comparative analysis of amino acid sequence and atomic resolution structure provides information on the prevalence of particular amino acids or a group of non-covalent interactions. Protein folding studies give the information about thermodynamic and kinetic stability in order to understand dynamic aspect of molecular adaptations. In this review, we have summarized information on amino acid sequence, structure, stability, and adaptability of α-amylases from different classes of extremophiles.

Keywords: Extremophile; Folding; Protein adaptation; Protein stability; α-Amylase.

Fig. 1

Structure of extremophilic α-amylases from psychrophilic, PDB ID 1AQH (Aghajari et al., 1998) (A); thermophilic, IBL1 (Machius et al., 1998) (B); hyperthermophilic, 4AEF (Park et al., 2013) (C); halophilic, 1WZA (Sivakumar et al., 2006) (D); acidophilic, 6GXV (Agirre et al., 2019) (E); and alkaliphilic microorganisms 1UD2 (Nonaka et al., 2003) (F)