9729178 Kumar The aim of this proposal is to develop strategies for the successful immobilization of proteins at solid surfaces. In this study, a-zirconium phosphonates with specific functionalities will be prepared, and selected proteins will be immobilized at these surfaces by covalent and non-covalent methods. Immobilized proteins will be examined with diffuse reflectance spectral methods (Ultraviolet-Visible, Fourier Transform InfraRed), powder X-ray diffraction, activity studies, and by differential scanning calorimetry. These data for the immobilized proteins will be compared with those of the free proteins to gain insight into how surface functionalities, linker lengths, and covalent immobilization influence bound protein behavior. Such detailed information is essential to learn how specific surfaces can be rationally designed in order to maximize the bound protein function. %%% The catalytic efficiency and selectivity of enzymes have not been fully exploited for societal needs due to their instability and high cost. Immobilized enzymes, on the other hand, are often more stable, result in lower costs, and they can be recycled. Immobilized proteins are important for applications involving biosensors, medical implants, enzyme reactors, and biomedical devices. Immobilized proteins can provide new and improved catalysts to produce fine chemicals, pharmaceutical intermediates, and synthetic fuels to meet growing societal needs while reducing the environmental impact of human activities. This activity is jointly supported by the Division of Chemistry, the Division of Materials Research, and the Office of Multidisciplinary Activities in the MPS Directorate. ***
