RESUMEN
A novel method of immobilizing cellulase on sodium alginate (SA)-polyethylene glycol (PEG) enabled the cellulase to be used repeatedly. The matrix of the immobilized cellulase was detected and characterized using Fourier transform infrared spectroscopy and scanning electron microscopy. In comparison with SA-immobilized cellulase, the relative enzyme activity and immobilization rate increased by 25% and 18%, respectively. The application range of the immobilized enzyme in terms of temperature and pH was larger than that of the free enzyme, and its thermal stability increased. The immobilized enzyme was used in enzymatic hydrolysis, in which MCC was used as the substrate. The optimal conditions for enzymatic hydrolysis were as follows: the dosage of SA-PEG-immobilized cellulase was 3.55 g/g total solids of the substrate, the concentration of the substrate was 13.16%, and the pH was 5.11. In comparison with the yield of reducing sugars in the first round of hydrolysis of MCC by SA-immobilized cellulase, the yield in the hydrolysis of MCC by SA-PEG-immobilized cellulase increased by 133%. After five cycles of repeated use, the total yield of reducing sugars when MCC was hydrolyzed by SA-PEG-immobilized cellulase was similar to that achieved with free cellulase. In comparison with the free enzyme, the highest yield when the immobilized enzyme was used was 22.68%. Therefore, the immobilized cellulase exhibited high performance in enzymatic hydrolysis.