An anisotropic glucose oxidasepolymer surfactant nanoconjugate is synthesized and shown to exhibit complex temperature-dependent phase behavior in the solvent-free state. At close to room temperature, the nanoconjugate crystallizes as a mesolamellar soft solid with an expanded interlayer spacing of ca. 12 nm and interchain correlation lengths consistent with alkyl tailtail and PEOPEO ordering. The soft solid displays a birefringent spherulitic texture and melts at 40 degrees C to produce a solvent-free liquid protein without loss of enzyme secondary structure. The nanoconjugate melt exhibits a birefringent dendritic texture below the conformation transition temperature (T-c) of glucose oxidase (58 degrees C) and retains interchain PEOPEO ordering. Our results indicate that the shape anisotropy of the proteinpolymer surfactant globular building block plays a key role in directing mesolamellar formation in the solvent-free solid and suggests that the microstructure observed in the solvent-free liquid protein below T-c is associated with restrictions in the intramolecular motions of the protein core of the nanoconjugate.