|Budget Amount *help
¥3,400,000 (Direct Cost : ¥3,400,000)
Fiscal Year 1998 : ¥600,000 (Direct Cost : ¥600,000)
Fiscal Year 1997 : ¥2,800,000 (Direct Cost : ¥2,800,000)
When cells and biological systems are exposed to lethal stresses, for example, heat stress, theyrespond to inducevarious latent functions, such as rapid synthesis of specific proteins including a set of heat shock proteins(HSPs), refolding of damaged proteins, translocation and release of proteins across membranes, formation of protein aggregates in an inert insoluble form etc.. These stress responsive or stimuli-responsive functions of cells, proteins, and membraneshave been quantitatively analyzed by the aqueous two-phase partitioning method etc. in the various levels and found to be triggered by the formation of the new transient structure between partly denaturedproteins and HSPs or cell membranes/liposomes, driven by the common principle of self-organIzation, and mediated by the transient hydrophobic Interaction among them. These functions have been successfully utilized for bio-production and bio-separation processes mainly integrating them with the stress induced self-assembled structure, such as stimuli-responsive polymers, aqueous two-phase systems (ATPS), and liposomes. When the cultivated cells or the protein mixture solution was exposed to the specific heat stress condition in the presence of liposomes, stimuli-responsive polymers and/or ATPS, the target protein could be trapped, refolded, translocated, and recovered selectively depending on the applied stress level and proteins.