Spectroscopic studies on the inhibitory effects of ionic liquids on lipase activity

•Interactions of lipase and ionic liquids were investigated by spectroscopic methods.•The activity of lipase decreases in the presence of ILs.•Fluorescence quenching mechanism of lipase depends on the types of the IL anions.•Hydrophobicity and hydrogen bonding are driven forces for IL–lipase interaction.

The effects of ionic liquids (ILs) on the lipase activity were studied by UV–Vis spectroscopy and the IL-lipase interaction mechanism at the molecular level was investigated by fluorescence technique. Experimental results indicated that the lipase activity was inhibited by ILs and the degree of inhibition highly depended on the chemical structures of ILs. The inhibitory ability of the Cl−- and Br−-based ILs increased with increasing the alkyl chain length in the IL cation. Thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS) were obtained by analyzing the fluorescence behavior of lipase with the addition of ILs. Both ΔH and ΔS were positive suggesting hydrophobicity was the major driven force for the Cl−- and Br−-based ILs. For the BF4−-, CF3SO3−-, ClO4−- and N(CN)2−-based ILs, hydrogen bonding was the main driven force. For a more comprehensive understanding of the effects of ILs on lipase activity, the roles of hydrophobicity and hydrogen bonding must be considered simultaneously. A regression-based equation was developed to describe the relationship of the inhibitory ability of ILs and their hydrophobicity and hydrogen bonding ability.

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