Ionic liquids (IL) gained interest due to their unique properties, notably their solvent capabilities and environmental friendliness. Their ability to dissolve proteins is of particular interest to bioorganic catalysis. Protein stability in IL varies depending on the nature of both protein and IL. Some enzymes are stabilized due to moderately and favorably altered secondary structures while suspended in IL, while others lose stability as a result of significant changes in structural conformation and permanent complexation between surface residues and components of the IL. The present study investigates the effect of transient exposure of cholesterol oxidase (ChO) to 1-ethyl-3-methylimidazolium tetrafluoroborate (emim-BF4) in the presence of flavin adenine dinucleotide (FAD), the prosthetic group of ChO. The activity and stability of the modified enzyme (ME) are compared to those of the starting enzyme and to those of a ME obtained in an alternate procedure using IL in the presence of water.

1-ethyl-3-methylimidazolium tetrafluoroborate used to “wire” cholesterol oxidase

243rd National Meeting (2012)

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