Extraction, purification, and functionality of proteins using deep eutectic solvents: a review

This review aims to study the overall impact of Deep Eutectic Solvents (DES) and Natural Deep Eutectic Solvents (NADES) on protein structure and function, exploring their effects on solubility, conformational stability, emulsifying properties, spinnability, and thermal stability based on the recently published articles. This structured approach clearly outlines significant findings regarding the impact of DESs and NADES on proteins structure and function with emphasis on their mechanisms. DESs and NADES can significantly influence protein structure through solvent–solute interactions that may stabilize or destabilize proteins depending on their components. Many proteins show enhanced solubility in DESs and NADES due to favorable interactions with the solvent’s hydrogen-bonding network. The effect of DES and NADES on thermal stability varies; while they may not inherently increase stability, they can provide protective environments against denaturation under certain conditions. Enzymes can maintain active in DES and NADES, although optimal conditions vary for each enzyme-substrate pair. There is a promising trend in the use of DES on an industrial scale, and a lot of research is being done for protein purification and separation of DES, as well as reducing extraction time with the help of new techniques to overcome its high viscosity and interfacial mass transfer resistance.