MgO-Fe3O4 linked cellulase enzyme complex improves the hydrolysis of cellulose from Chlorella sp. CYB2
Rajendran Velmurugan, Aran Incharoensakdi
Biochemical Engineering Journal
In the present study, a novel catalyst was prepared by combining cellulase enzyme complex with metal oxides as a substrate activating and enzyme stabilizing component. The cellulose content obtained from Chlorella sp. CYB2 was treated with magnetic metal oxide linked enzyme complex through xylan aldehyde linking molecule. In order to improve the hydrolysis process, MgO was blended with Fe3O4 and the resulting complex had significant improvement in immobilization yield, activity recovery and hydrolysis of cellulose. Addition of xylan aldehyde as a linking molecule enhanced the enzyme binding onto metal nanoparticle. The results on hydrolysis showed the reduction in crystallinity of cellulose corresponding to the increase in enzymatic digestibility of cellulose. Under optimized conditions, the glucose yield obtained was 91% of theoretical maximum. The enhancement in hydrolysis is correlated with the degradation of large molecule into well accessible substrate assisted by the action of metal oxides.
Circular dichroism, Secondary structure, Nanostructures, Biochemistry, Materials