Assays with 2009 Influenza A Virus and other seasonal influenza viruses are performed biosafety level-2, whereas assays with replication competent wide-type H5N1 and other potentially pandemic viruses must be performed under biosafety level-3 containment, requiring convenient and laborsaving assays to minimize the hands-on steps. Conventional virus quantification and neutralization tests for influenza viruses require several manipulations, which are laborious and rather slow. However, the RTCA assay provides data continuously and automatically in a remote manner after the initial virus inoculation, which could save on time and labor for assay development and also decrease the risk of aerosol generation. With the few hands-on manipulations required, this new format allows for label-free, high throughput, and automatic testing, and could easily be adapted to assays under BSL-3 conditions. The encapsulation of biomolecules, such as enzymes, antibodies, and other proteins as well as whole cells, on porous materials is an important Nifedipine approach to stabilize the biological components in what is often an unnatural environment while retaining their functions and activities. However, there still exist a series of technical bottlenecks for practical applications of immobilized enzymes, such as low catalytic activity, restricted mass transfer, enzyme leaching upon reuse, and sophisticated and expensive synthesis procedures. Taking into consideration all these factors, nanoporous gold, fabricated by a simple dealloying method, was selected here as a support for enzyme immobilization due to its unique physicochemical properties. NPG has tunable pores at a nanometer scale that could fit proteins with different molecular weights and dimensions and offer the possibility of adsorbing or entrapping biomolecules within the pores as well as on the external surfaces depending on the nature of the proteins. In addition, NPG is intrinsically a nanostructured bulk material, thus it can be easily employed and recovered for reuse. Moreover, NPG has a biocompatible and active surface, which offers the opportunity for covalent binding through for example the well known thiol-based self-assembled Ginsenoside-Rb3 monolayer technology. The aim of enzyme immobilization is to maintain the catalytic activity whilst improving its stability and ease of reuse. In this study, we constructed the enzyme-NPG biocomposites by assembling various enzymes onto the surface of NPG. It was clearly observed that the resulted enzyme-NPG biocomposites demonstrated not only remarkable catalytic performance but also excellent reuse stability compared with free enzymes. These results are superior to those reported in literatures. Excellent catalytic performance alone is not enough to ensure a high stability under different conditions. The stability of enzyme plays a key role during the practical use of enzyme.