Caracterização Bioquímica de endoglucanase produzida por fungo filamentoso Pycnoporus sanguineus

Abstract

The cellulolitic complex is made up by enzymes that act synergistically on the cellulose molecule, having as its end product glucose monosaccharides. The endoglucanase enzyme, also known as CMCase, internally cleaves cellulose reducing the grade of polymerization of this molecule and exposing reducing and non-reducing ends. The major industrial interest of these enzymes is the production of ethanol from the degradation of plant biomass, called second generation ethanol. However, there are other industrial applications in these enzymes, such as in the juice, winemaking and animal feed industry. The aim of this work was to characterize the endoglucanase produced by the mesophyll filamentous fungus Pycnoporus sanguineus. Optimum pH of enzyme activity was 5.0. The enzyme maintained more than 80% of its original activity and structural stability in the pH range 3.0-8.0. The optimal endoglucanase temperature was 70°C, and after 1 hour of incubation, more than 80% of its activity and structural stability after incubation for 1 hour at 60°C. High structural stability is not often found for endoglucanases produced by mesophilic fungi. Thus, it is possible to infer that the enzyme analyzed in the present work presents desirable characteristics for industrial application, considering its ability to remain stable over a wide pH range and at high temperatures.