Partial Purification of Cellulase Enzyme from Fusarioum oxysporium by Using Egg White Matrix

Aim: Protein matrix possesses a capacity to bind organic and inorganic matter. Egg white matrix as an adsorbent was utilized for partial purification of cellulase enzyme in detailed batch study.

Methodology: Effect of pH, matrix size, enzyme concentration, contact time and temperature on the binding of cellulase on egg white matrix was studied. Desorption studies was carried with variable pH, sodium chloride and ammonium sulphate system to desorbs the cellulase for the egg white matrix.

Results: Equilibrium isotherms for the adsorption of the cellulase enzyme on egg white matrix were well fitted to Freundlich and Langmuir isotherm models. The adsorption process has been found endothermic in nature and thermodynamic parameters, Gibb’s free energy (∆Gº), change in enthalpy (∆Hº) and change in entropy (∆Sº) have been calculated as -13276.21, 2025.47 and 698.64 (KJ mol-1) respectively. Thermodynamic studies revealed that the adsorption process is spontaneous and endothermic in nature. In desorption studies it was concluded that maximum elution (66.8% was obtained for cellulase enzyme with 0.3M (NH4)2SO4 with respect to different pH and sodium chloride solution. Cellulase enzyme obtained after desorption process has maximum purification fold of 4.25 with 60% recovery.

Conclusion: The results from the current research suggest that egg white can be used for partial purification of cellulase enzyme with less cost.