Extremophilic Ligninolytic Enzymes: Versatile Biocatalytic Tools with Impressive Biotechnological Potential

Extremophilic microbial communities have developed several physiological and molecular strategies to survive and grow in extreme environments. This review explores the adaptive mechanisms of extremophilic ligninolytic enzymes such as laccase, lignin peroxidase (LiP), and manganese peroxidase (MnP). The extremophilic ligninolytic enzyme adaptive features such as different compositions of amino acids, hydrophobic interaction, surface charges, tighter packing (compactness), a deleted loop, saturated/unsaturated fatty acid, salt bridge, disulfide bridge, hydrogen bond, several ions, and alpha-helical, as well as, cysteinyl-tRNA synthetase enzyme to maintain their active stability for catalytic functionalities in extreme conditions. The biochemical properties of extremophilic laccase are monomeric, dimeric, and trimeric glycoprotein with a molecular weight range of 50 to 97 kDa, while glycosylated haem proteins, LiP, and MnP, display a molecular weight ranging from 38 to 62.5 kDa (LiP: 38-46 kDa; MnP: 38-62.5 kDa). The optimum activity of laccase in bacteria and fungus was noted at pH 4.0-10.0. Moreover, the exquisite LiP and MnP activities in fungus occurred at pH 3.0-5.0, while bacteria adopted the diverse range of pH 4.0-9.0. Finally, concluding remarks, the current research needs to highlight the emerging applications of ligninolytic enzymes in broad range of industrial and biotechnological potentials. [GRAPHICS] .

Automated summary

This review explores the adaptive mechanisms of extremophilic microbial communities and extremophilic ligninolytic enzymes, as well as their biochemical properties and activity. The research emphasizes the emerging applications of ligninolytic enzymes in a broad range of industrial and biotechnological potentials.