Nordwald_2015_Chembiochem_16_2456

Reference

Title : Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure - Nordwald_2015_Chembiochem_16_2456
Author(s) : Nordwald EM , Plaks JG , Snell JR , Sousa MC , Kaar JL
Ref : Chembiochem , 16 :2456 , 2015
Abstract : We present the first crystallographic insight into the interactions of an ionic liquid (IL) with an enzyme, which has widespread implications for stabilizing enzymes in IL media for biocatalysis. Structures of Bacillus subtilis lipase A (lipA) and an IL-stable variant (QM-lipA) were obtained in the presence of increasing concentrations of 1-butyl-3-methylimidazolium chloride ([BMIM][Cl]). These studies revealed that the [BMIM] cation interacts with surface residues through hydrophobic and cation-pi interactions. Of specific interest was the disruption of internal stacking interactions of aromatic side chains by [BMIM], which provides structural evidence for the mechanism of enzyme denaturation by ILs. The interaction of [BMIM] and Cl ions with lipA was reduced by the stabilizing mutations Y49E and G158E in QM-lipA. Ultimately, these findings present the molecular basis for stabilizing enzymes from IL-induced inactivation, as well as the selection of ILs that are less denaturing.
ESTHER : Nordwald_2015_Chembiochem_16_2456
PubMedSearch : Nordwald_2015_Chembiochem_16_2456
PubMedID: 26388426
Gene_locus related to this paper: bacsu-lip

Related information

Gene_locus related to this paper: bacsu-lip

Citations formats

Nordwald EM, Plaks JG, Snell JR, Sousa MC, Kaar JL (2015)
Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure
Chembiochem 16 :2456

Nordwald EM, Plaks JG, Snell JR, Sousa MC, Kaar JL (2015)
Chembiochem 16 :2456