Lipases solvent engineering

Bellot, J.C., Choisnard, L., Castillo, E., and Marty, A. 2001. Combining solvent engineering and thermodynamic modebng to enhance selectivity during monoglyceride synthesis by lipase-catalyzed esterification. Enz. Microb. Technol. 28 362-369. 

The structure of lipases has been shown to be similar in both water and hydrophobic solvents and binding of solvent molecules other than water has been observed. Rates of reaction and enantioselectivity have been altered by changing the solvent in a process called solvent engineering. 

Lipases are able to work in very different media. They work in biphasic systems and in monophasic (in the presence of hydrophilic or hydrophobic solvents) systems where the water content can vary significantly between aqueous and anhydrous media. They have been tested also in ionic liquid media (Lau et al. 2000 Wasserscheid and Keim 2000 Kamal and Chouhan 2004 Ha et al. 2007), in supercritical fluids (Laudani et al. 2007) and in gaseous media (Cameron et al. 2002). The different media for enzymatic catalysis has been outlined before (see section 1.6) and it will not be further discussed here. However, some examples of modulation of activity and selectivity of lipases by medium engineering will be described in this section. 

Moniruzzaman, M., Hayashi, Y., Talukder, M.M.R., Saito, E., Kawanishi, T. 2006. Effect of aprotic solvents on the enzymatic activity of lipase in AOT reverse micelles. Biochem. Engin. J. 30, 237-244. 

Lee KH, Park C-H Lee EY. 2010. Biosynthesis of glycerol carbonate from glycerol by lipase in dimethyl carbonate as the solvent. Bioprocess and Biosystems Engineering 33(9) 1059-1065. 

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