Fig. 5: Thermal stability of CALB in different IL microenvironments. | Nature Communications

Fig. 5: Thermal stability of CALB in different IL microenvironments.

From: Engineering enzyme conformation within liquid-solid hybrid microreactors for enhanced continuous-flow biocatalysis

Fig. 5

a, b Comparisons of the temperature-dependent enzymatic activity within different IL microenvironments using 1-phenylethyl alcohol as a substrate: a [PEG600 (mim)2][NTf2]2, b [EMIM]NTf2. c Specific activity of CALB in different IL microenvironments. Reaction conditions: 3.0 g hybrid catalyst, 1-phenylethyl alcohol (0.80 or 0.10 M) and vinyl acetate (3.20 or 0.40 M) in n-octane, flow velocity 2.0 mL h−1. d CD spectra of CALB at different temperatures in various mediums. e Time evolution of RMSD for CALB in [PEG600 (mim)2][NTf2]2 and [EMIM]NTf2 with temperature switching from 30 oC (0-300 ns) to 80 oC (300-600 ns) in three independent simulations. f, g Secondary structures of α-helix and β-sheet for CALB in [PEG600(mim)2][NTf2]2 or [EMIM]NTf2 at temperatures of 30 oC and 80 oC. h, i Snapshots in the vicinity of CALB with [PEG600(mim)2][NTf2]2 or [EMIM]NTf2 as a medium at late times (at 600 ns on run−1). Only a portion of the simulation box is shown for clarity in (h) and (i), PEG groups are shown in cyan, NTf2 ion is shown in iceblue, and substrate molecules are hidden.

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