Can new reactions be carried out in nonpolar solvents?
The quick answers is yes, since reactions in aqueous solutions can be unfavorable due to low Keq’s, side reactions, or insolubility of reactants. Consider lipases which cleave fatty acid esters by hydrolysis in aqueous solutions. In nonaqueous solutions, reactions such as transesterification or ammonolysis can be performed. Enzymes are clearly active in organic solvents which appears to contradict our central concepts of protein stability. Two reasons could could explain this stability. • It is possible that from a thermodynamic view, the enzyme is stable in organic solvents. However, as was discussed above, this is inconceivable given the delicate balance of noncovalent and hydrophobic interactions required for protein stability. • The second reason must win the day: the protein is unable to unfold from a kinetic point of view. Conformational flexibility is required for denaturation. This must require water as the solvent. A specific example helps illustrate the effects of different s
