(620cf) Co-Immobilization of Cellulase Complex on Magnetic Nanoparticles Aiming to Sugarcane Bagasse Hydrolysis

Authors: 
França, Í. W. L. Sr., Universidade Federal do Ceará
Goncalves, L. R. B., Universidade Federal do Ceará

Second-generation bioethanol produced from lignocellulosic biomass are a potential alternative to fossil fuels due to its renewability, low environmental impact, and limited employment of food crops. Compared to traditional chemical processes, the enzymatic hydrolysis of lignocellulosic biomass usually involves lower energy consumption, milder reaction conditions, substrate specificity and also achieving higher yields. High yields in the conversion of cellulose into glucose, used as substrate to bioethanol production, may be achieved by using cellulases, the enzymes able to hydrolyze β-1,4 linkages in cellulose chains, by the synergetic action of three main types: endoglucanases, exoglucanases and β–glucosidase. Although the advantages of second-generation bioethanol, its final commercialization must overcome primary costs, for instance, due to enzyme. A reduction in the cost of enzymatic hydrolysis of lignocellulosic biomass might be achieved by the development of a process that recover/reuse the enzyme. For this enzyme recycling process, some strategies have been proposed: enzyme ultrafiltration, enzyme re-adsorption, recycle for solids and liquids after hydrolysis, surfactant (or other enzyme coagulant agent) addition and enzyme immobilization. The use of magnetic materials as enzyme immobilization carries may be an interesting alternative since it is easy to separate, recover and reuse. The immobilized cellulases might be magnetically separated, recovered and reused in a new cycle of enzymatic hydrolysis. Therefore, the aim of this work was to evaluate the possibility of immobilizing cellulases on magnetic particles in order to enable enzyme re-use on the hydrolysis of sugarcane bagasse, a very abundant biomass in Brazil. The magnetic particles (iron oxide) were active by Glutaraldehyde at room temperature and pH 4.8. The enzyme (celullase from Trichoderma reeseiSigma Aldrich) was maintained of citrate buffer (50mM; pH 4.8). The activity of cellulose was measured individually for each enzyme in the complex, as well the total celullase activity. Preliminary results showed the stability of the support prepared for the immobilization procedure, and the possibility of its magnetic recovery after the hydrolysis of sugarcane bagasse.