| 초록 |
In order to stabilize beta-glucosidase, surface display system was newly adopted because the surface display is one of the c-terminal specific immobilization method and is expected to be effective in overcoming the recombinant protein deactivation. To immobilize beta-glucosidase protein on the cell wall surface of S. cerevisiae, the beta-glucosidase gene was fused with the c-terminal half of alpha-agglutinin gene. Constructed vectors, pBGL-AG (surfae-display)and pBGL (secretion) was introduced into S. cerevisiae L2612 by electroporation method. The transforments were named as L2612(pBGL-AG) and L2612(pBGL) The surface-displayed yeast, L2612(pBGl-AG) showed beta-glucosidase activity prevalently in cell pellet and cell wall fraction. In contrast, the secreting yeast, L2612(pBGL) showed the activity only in culture medium. The beta-glucosidase activity of L2612(pBGL-AG) was higher and more stable than that of L2612(pBGL). Novel surface-engineered cellobiose-utilizing yeast was applied to ethanol production from cellobiose and glucose mixtureThe cellobiose usage of L2612(pBGL-AG) shows about 10% increase compared with L2612(pBGL) |
