Carbon dioxide capture and storage in geological formations is recognized as a promising method for decoupling fossil fuel use and carbon emissions. Carbon dioxide injected into geological formations is expected to be trapped by several mechanisms against buoyancy. In this paper, we focused on capillary rapping. Trapped bubbles in packed beds of glass beads were visualized by means of micro-focused X-ray CT at pore scale for supercritical CO 2 and water systems at reservoir condition and for nitrogen and water systems at laboratory room condition. When the diameter of glass beads is the same, distribution of volume of trapped bubbles is similar for each condition. At the pressure of 8.5MPa and the temperature of 45ºC, which corresponds to just above a critical point, the morphology of the interface between the supercritical CO 2 and water suggests that CO 2 is non-wetting to glass beads. Residual gas saturation increases with a decrease in a diameter of glass beads, because the capillary pressure is higher with respect to buoyancy. Residual gas saturation can be expressed as a function of the reverse Bond number for each condition. Distribution of trapped bubble volume is identical with each other for each condition at same diameter of glass beads. The large trapped bubbles contribute to the residual gas saturation.

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Biomolecules such as protein, peptide and nucleic acids interact with each other in the cell controlling its life activities. Therefore, techniques to reproduce biomolecular interactions correctly on the solid substrate would be a good versatile way to clarify the biological phenomena. In this research, we investigated the influence of protein orientation and density on peptide-protein interaction (adopting cysteine synthase (CS) complex formation as the model) detection with employing site specific protein immobilization technique. As the results, consideration of the location of functional site with avoiding the steric hindrance by adjusting the protein density and the degree of freedom of the peptide would be important to design higher interaction detection system. We aim to develop a new strategy of protein design based on the phage display and single-molecule sorting. In the first step of the method, a library of phages expressing a target protein with randomized sequence is prepared. In the second step, the expressed proteins are labeled by fluorophore(s) and are sorted based on the fluorescence signals from single phages. To realize the strategy, we prepared a phage expressing C-terminal fragment (214-230) of GFP. The addition of the N terminal fragment (1-214) of GFP, purified separately, to the phage caused the reconstitution of GFP and the appearance of the fluorescence signal. We are currently conducting the observation and sorting of the phages having the reconstituted GFP on the surface. 2P086 無機基板表面を標的としたラクダ抗体から着想するスマート なバイオセンサー仕様抗体の設計