부산대학교 도서관

The study was targeted to saccharify foodwastes with the cellulolytic and amylolytic enzymes obtained from culture supernatant ofTrichoderma harzianumFJ1 and analyze the kinetics of the saccharification in order to enlarge the utilization in industrial application.T. harzianumFJ1 highly produced various cellulolytic (filter paperase 0.9, carboxymethyl cellulase 22.0, β-glucosidase 1.2, Avicelase 0.4, xylanase 30.8, as U/mL-supernatant) and amylolytic (α-amylase 5.6, β-amylase 3.1, glucoamylase 2.6, as U/mL-supernatant) enzymes. The 23–98 g/L of reducing sugars were obtained under various experimental conditions by changing FPase to between 0.2–0.6 U/mL and foodwastes between 5–20% (w/v), with fixed conditions at 50°C, pH 5.0, and 100 rpm for 24 h. As the enzymatic hydrolysis of foodwastes were performed in a heterogeneous solid-liquid reaction system, it was significantly influenced by enzyme and substrate concentrations used, where the pH and temperature were fixed at their experimental optima of 5.0 and 50°C, respectively. An empirical model was employed to simplify the kinetics of the saccharification reaction. The reducing sugars concentration (X, g/L) in the saccharification reaction was expressed by a power curve (X=K·tn) for the reaction time (t), where the coefficient,Kandn, were related to functions of the enzymes concentrations (E) and foodwastes concentrations (S), as follow:K=10.894 Ln(E·S2)-56.768,n=0.0608·(E/S)−0.2130. The kinetic developed to analyze the effective saccharification of foodwastes composed of complex organic compounds could adequately explain the cases under various saccharification conditions. The kinetics results would be available for reducing sugars production processes, with the reducing sugars obtained at a lower cost can be used as carbon and energy sources in various fermentation industries.