ABSTRACT
Charge storage devices with high energy density and enhanced rate capabilities are highly sought after in today's mobile world. Although several high-rate pseudocapacitive anode materials have been reported, cathode materials operating in a high potential range versus lithium metal are much less common. Here, we present a nanostructured version of the well-known cathode material, LiMn2O4. The reduction in lithium-ion diffusion lengths and improvement in rate capabilities is realized through a combination of nanocrystallinity and the formation of a 3-D porous framework. Materials were fabricated from nanoporous Mn3O4 films made by block copolymer templating of preformed nanocrystals. The nanoporous Mn3O4 was then converted via solid-state reaction with LiOH to nanoporous LixMn2O4 (1 < x < 2). The resulting films had a wall thickness of â¼15 nm, which is small enough to be impacted by inactive surface sites. As a consequence, capacity was reduced by about half compared to bulk LiMn2O4, but both charge and discharge kinetics as well as cycling stability were improved significantly. Kinetic analysis of the redox reactions was used to verify the pseudocapacitive mechanisms of charge storage and establish the feasibility of using nanoporous LixMn2O4 as a cathode in lithium-ion devices based on pseudocapacitive charge storage.
ABSTRACT
We report a new material design concept for synthetic, thermally responsive poly(N-isopropylacrylamide)-based copolymer nanoparticle (NP) hydrogels, which protect proteins from thermal stress. The NP hydrogels bind and protect a target enzyme from irreversible activity loss upon exposure to heat but "autonomously" release the enzyme upon subsequent cooling of the solution. Incorporation of the optimized amount of negatively charged and hydrophobic comonomers to the NP hydrogels was key to achieve these desired functions. As the NP hydrogels do not show a strong affinity for the enzyme at room temperature, they can remain in solution without adversely affecting enzymatic activity or they can be removed by filtration to leave the enzyme in solution. The results demonstrate the promise of this approach for improving the thermal tolerance of proteins.
