期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 238, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2023.124051
关键词
Extremophiles; Non aqueous enzymes; Solvent stability; Immobilization; Adaptations
Nonaqueous enzymology has unique possibilities in bio-catalysis, but the presence of solvents often hinders enzyme catalysis. Information about solvent-stable enzymes is scarce, yet these enzymes have great value in biotechnology. Extremophiles, particularly those with inherent structural attributes, can be a valuable source for studying solvent-stable enzymes. Protein engineering approaches are used to enhance catalytic flexibility and stability under non-aqueous conditions. This review provides a comprehensive overview of solvent-stable enzymes from extremophilic microorganisms and discusses strategies for optimal immobilization and catalysis.
Non-aqueous enzymology has always drawn attention due to the wide range of unique possibilities in bio-catalysis. In general, the enzymes do not or insignificantly catalyze substrate in the presence of solvents. This is due to the interfering interactions of the solvents between enzyme and water molecules at the interface. Therefore, information about solvent-stable enzymes is scarce. Yet, solvent-stable enzymes prove quite valuable in the present day biotechnology. The enzymatic hydrolysis of the substrates in solvents synthesizes commer-cially valuable products, such as peptides, esters, and other transesterification products. Extremophiles, the most valuable yet not extensively explored candidates, can be an excellent source to investigate this avenue. Due to inherent structural attributes, many extremozymes can catalyze and maintain stability in organic solvents. In the present review, we aim to consolidate information about the solvent-stable enzymes from various extremophilic microorganisms. Further, it would be interesting to learn about the mechanism adapted by these microorganisms to sustain solvent stress. Various approaches to protein engineering are used to enhance catalytic flexibility and stability and broaden biocatalysis's prospects under non-aqueous conditions. It also describes strategies to ach-ieve optimal immobilization with minimum inhibition of the catalysis. The proposed review would significantly aid our understanding of non-aqueous enzymology.
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