Cellulose is the most abundant renewable carbon source in the world. Presently the conversion of pre-treated biomass to ethanol is done in three stages: production of saccharolytic enzymes (cellulases and hemi cellulases), enzymatic hydrolysis of the carbohydrate components present in pre-treated biomass to sugars, and fermentation of the released sugars. These processes occur in a single step in a process arrangement called consolidated bioprocessing (CBP), where saccharolytic enzyme production, hydrolysis and fermentation are carried out by a single microbe or a mixed stable culture. Our goal is to engineer a CBP competent S. cerevisiae strain by heterologously expressing fungal cellulase genes. We are cloning endoglucanases (EGs) from different fungi and studying their heterologous expression in yeast. All genes were PCR amplified from either genomic DNA or cDNA and cloned into a yeast expression vector that directs expression using a constitutive promoter. Genes that expressed active secreted endoglucanase were identified using Congo red indicator plates. The ability of the expressed endoglucanases to hydrolyze various cellulosic substrates was investigated using the bicinchoninic acid assay. Five endoglucanaes were found to be functionally expressed at levels ranging from 1µg/ml to 4µg/ml. This level of expression is about the same level of Cel5A, formerly called EG2, present in a commercial cellulase system preparation that hydrolyses 0.5% PASC in 70 hours. Future efforts at producing a CBP competent yeast will therefore be directed at increasing levels of endoglucanase expression, and introducing exoglucanase and β-glucosidase genes into the endoglucanase expressing yeast.