Celluloses are hydrolyzed to cellooligosaccharides by endoglucanases and exoglucanases, and then â-glucosidase degrades them to glucose sequentially. Bacterial multi-enzyme complex, the so called cellulosome, have very high activity on crystalline cellulose. A cellulosome contains scaffolding subunit which consists of cellulose-binding domain and cohesion domain. The nine cohesion domains interact with docking domain of active cellulases. Hence, reconstruction of cellulosome like complex will enhance the synergistic effect of cellulases. The catalytic subunits such as CelA, CelS, and â-glucosidase and non-catalytic subunit, CipA, genes are prepared from C. thermocellum S-7 (ATCC 31924) and C. cellulolyticum H10 (ATCC 35319). The multi-scaffolding subunits are displayed on the cell surface fused to PgsA anchor protein. Three extracellular cellulases bind to the scaffolding chain. This whole-cell biocatalyst, by displaying multi-cellulosome like complex on the surface of the ethanologenic bacteria such as E. coli LY01 and Z. mobilis, enables direct ethanol production from cellulose.