Cellulase can hydrolyze cellulose to produce reducing sugars such as cellobiose and cellotriose. β-glucosidas can further hydrolyze cellobiose and cellobiose produced by cellulase to produce glucose. According to the hydrolysis mechanisms of cellulase and β-glucosidas, we selected two enzyems, cellulase and β-glucosidase to study optimization of co-immobilization of cellulase and β-glucosidas. Meanwhile, we selected two materials, activated carbon and sodium alginate to co-immobilize cellulase and β-glucosidas by the immobilization method of embedding-adsorption. The immobilization conditions, alginate, CaCl2 and activated carbon was optimized. The results showed that the optimum concentrations of sodium alginate and CaCl2 were 2% and 2%, respectively, and the quality of activated carbon is 0.15 g. The optimal ratio of cellulase to β - glucosidase was 1:1.5. The results indicated that cellulase and β-glucosidase had a synergistic effect and that their compound degradation of cellulose was better than the separate effects of the two enzymes acting independently.

In this study, we successfully isolated a strain of Aspergillus oryzae TR08, which produced xylanase secreted to the outside of the cell productively. The enzyme activity and specific activity in the fermentation broth of this strain reached peak values of 451 IU/mL and 1963 IU/mg after 156 h of fermentation. A single factor experiment was designed, and it was found that the strain was adjusted to the initial pH of the fermentation broth to 7.5 in a shaker at 180 rpm and 32 °C. After 156 h of fermentation, the enzyme activity reached a maximum of 1264 IU/mL. The optimal reaction temperature and pH value of the xylanase were 55 °C and 7.5, respectively, and it had excellent acid and alkali resistance and a wide pH activity range. The xylanase was increased the catalytic activity by 15% in 0.25 mM Fe3+, and the biological activity of the enzyme was not affected in the sodium dodecyl sulfate environment.