Enzymatic Reactions using Ionic Liquids for Green Sustainable Chemical Process; Stabilization and Activation of Lipases

Abstract

The enzymatic reaction is highly respected from an environmentally‐friendly point‐of‐view. Optimization of the reaction media and supporting materials of enzymes must be investigated in parallel with the effort to develop new enzymes. Lipases are frequently used for organic syntheses as synthetic tools even industry because of their acceptance of having a broad range of substrates, stability, and availability. We have investigated the possibility of ILs as both a solvent and activating or stabilization agent of enzymes, in particular, lipase as a model enzyme. ILs allowed recyclable use of a lipase and significant acceleration of transesterification, and also enhanced the stability and reaction activity of a lipase by immobilization through a lyophilization process. We discuss how we enhanced the enzyme capability using the IL engineering focusing on lipase‐catalyzed reactions, i. e., realization of the recyclable use of an enzyme, how ILs mediated the enhanced reaction rate, and improved the stability of the enzyme.

Amylase production from marine sponge Hymeniacidon perlevis; potentials sustainability benefits

“…Various researchers have proposed enzyme-mediated reactions as the key to green and sustainable chemistry [ 36 ]. Enzyme from marine microorganisms is a better way forward for a green and sustainable enzyme-mediated production process.…”

Ionic Liquids in Metal, Photo-, Electro-, and (Bio) Catalysis

“…Hydrolases accept a wide variety of substrates while maintaining their regioselectivity and stereoselectivity, as shown in Figure . The excellent properties of ILs as reaction media for lipase-catalyzed synthetic reactions have been widely reviewed, ,− as demonstrated in Table , which shows numerous representative examples of lipase-catalyzed reactions in IL-based systems. Proteases, such as trypsin and chymotrypsin, function as serin-hydrolases, while others like papain are thiol-hydrolases.…”

Ionozymes for Efficient Synthesis of Cadaverine: Offering a Sustainable Way for Bio-nylon 5X Production

“…More recently, the fourth-generation ILs, based on the unique properties of IL mixtures including the IL–water, IL–IL, IL–deep eutectic solvents (DES), and so on, have been proposed to have distinct and unexpected effects on the enzymatic reaction. , The enzymatic reaction systems with a specific IL microenvironment are defined as “ionozyme” . The ionozyme system mainly tries to improve some specific properties of enzymes in the unique ionic microenvironment, such as increasing substrate solubility, improving substrate affinity, boosting the enzymatic activity or stability by modifying the enzymatic catalytic pocket, or changing the binding mode with cofactors. − Ji et al developed a novel ionozyme strategy for efficient bioconversion of CO 2 by combining newly discovered formate dehydrogenase FDHPa with the IL synergetic system. The ionozyme (FDHPa-[Ch]­[Pro]-[TMG]­[PhO]) improved 142.3-fold in CO 2 conversion over commercial FDHCb in the conventional low salt buffer.…”