Preliminary study on enzyme activity of changes recombinant cellulase E4

Cellulose E4 is a special cellulase from Thermomonospora fusca, which has relatively high activity on bacterial microcrystalline cellulose (BMCC) and synergizes with both classes of exocellulases and with endocellulases, but the other endocellulases from T. fusca do not synergize with each other. Initial studies showed that different substrate hydrolysis activity had a great relationship with binding domain (CBD). So we deleted the CBD and constructed four groups of recombinant plasmids, transferred them to the yeast GS115 expression system, to get the corresponding recombinant protein. The results showed that the deletion of the CBD had an effect on the temperature, pH stability, and different substrate degradation vitality. And reveal the complexity of the cellulase degradation mechanism.