An extracellular xylanase from the thermophilic fungus Melanocarpus albomyces IIS 68 was evaluated for its activity and stability in the presence of polyols and salts at 60 °C, and found to be an effective protecting agent for thermal deactivation of enzyme. Response surface methodology was employed to study the synergistic effects of glycerol and NaCl (thermostabilizers) for xylanase stability. The addition of these thermo-stabilizers resulted in more than a 10-fold increment in enzyme half-life. Activation energy (Ea) and thermodynamic parameters such as ∆H, ∆G, and ∆S were calculated for the thermal inactivation of free and immobilized xylanase. The immobilized enzyme underwent substantially less conformational changes because of its enhanced stability and increased compactness, providing better thermo-stability at elevated temperatures. These findings suggest that the combined effect of glycerol and sodium chloride serves as a potential stabilizer for extracellular thermophilic xylanase, which finds commercial application in many industries, especially in the pulp and paper industry.
Class I cellobiose dehydrogenases (CDHs) are extracellular hemoflavo enzymes produced at low levels by the Basidiomycetes (white rot fungi). In presence of suitable electron acceptors, e.g., cytochrome c, 2,6-dichlorophenol-indophenol, or metal ions, it oxidizes cellobiose to cellobionolactone. A stringent requirement for disaccharides makes CDH also useful for conversion of lactose to lactobionic acid, an important ingredient in pharma and detergent industry. In this work, class I CDH was produced using a newly identified white rot fungus Termitomyces sp. OE147. Four media were evaluated for CDH production, and maximum enzyme activity of 0.92 international unit (IU)/ml was obtained on Ludwig medium under submerged conditions. Statistical optimization of N source, which had significant effect on CDH production, using Box-Behnken design followed by optimization of inoculum size and age resulted in an increase in activity to 2.9 IU/ml and a productivity of ~25 IU/l/h. The nearly purified CDH exhibited high activity of 26.4 IU/mg protein on lactose indicating this enzyme to be useful for lactobionic acid synthesis. Some of the internal peptide sequences bore 100 % homology to the CDH produced in Myceliophthora thermophila. The fungal isolate was amenable to scale up, and an overall productivity of ~18 IU/l/h was obtained at 14-l level.
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