In this work a facile method for fabricating protein‐sequestered liquid crystal (LC) emulsion droplets based on the uptake of surface‐engineered protein–polymer surfactant (PS) core–shell bioconjugates is described. Uptake of myoglobin‐PS, bovine serum albumin‐PS, Zn‐porphyrin myoglobin‐PS, horseradish peroxidase‐PS, and glucose oxidase‐PS occurs without structural or functional degradation, and gives rise to sequestration within the interior or at the surface of 4‐cyano‐4′‐pentylbiphenyl (5CB) nematic droplets depending on the surface modification of the protein‐PS bioconjugates. Differences in uptake behavior are used to achieve the spontaneous positional assembly of multiple proteins in the LC phase, and the use of spatially separated glucose oxidase‐PS and horseradish peroxidase‐PS bioconjugates is demonstrated to produce 5CB based droplets capable of housing an enzyme cascade reaction. This method opens a pathway for the development of bioactive liquid crystal droplets and can have potential applications in the optical sensing of biomolecular substrates.

A solvent-free porous liquid comprising polymer-surfactant modified hollow silica nanorods shows significant CO2 adsorption at 0 °C.

Integration of molecular liquid crystals (LCs) with functional proteins can provide new class of materials for potential applications in optical biosensing. However, hydrophobic nematic LCs (length ∼ 1−2 nm) and hydrophilic proteins, size ∼ O (nm), do not intermix without chemical modification of at least one of them. Bioconjugation of proteins with a polyethylene glycol-based polymeric surfactant (PS) can provide a core−shell system that is sequestered within nonaqueous LC (4-cyano-4′-pentylbiphenyl) microdroplets. However, the nature of interactions between the components and detailed understanding of the resultant hybrid microstructure remains unclear.Here, using a combination of isothermal titration calorimetry (ITC), fluorescence microscopy, and infrared-imaging spectroscopy, we show that strong hydrophobic interactions between the LC and PS drives the sequestration of a myoglobin−PS (Mb−PS; dispersed in the aqueous phase) into the LC spherical microdroplets or even into a bulk LC phase. The average values of both, the binding constant and the standard molar enthalpy change, are increased by approximately a factor of 2.5 times when the unmodified Mb is conjugated to the PS. Small-angle X-ray scattering studies reveal that LC molecules act as a solvent for the Mb−PS conjugate; furthermore, the LC long-range order is disturbed due to mixing, as exemplified by the change in its coherence length from 8.9 to 5.7 nm. Detailed allatomistic molecular dynamic simulations for a three-component PS−water−LC system show a change in interaction energy of −144 kJ mol −1 PS −1 upon the contact of PS chains (initially dispersed in water) with LC and agree with the ITC experiments.