Immobilization of xylanase on modified grafted alginate polyethyleneimine bead based on impact of sodium cation effect.

Alginate- polyethyleneimine gel beads modified by using 0.3 M Na+ were used for covalent immobilization of Aspergillus flavus xylanase. SEM images showed distorted structure with addition of Na+ that impaired the egg-box structure formation offered much covalent binding with xylanase. Immobilization onto (Alg+PEI/Na+) showed an enhancement in the operational stability, immobilization efficiency as well as immobilization yield. Covalent immobilization of xylanase onto (Alg+PEI/Na+) enhanced xylanase activity over a wide range of pHs (4–5.5) comparable to its free formula. As well as an increase in reaction temperature up to 60°C. However, immobilized formula of enzyme showed abroad thermal stability that it retained 79.0% of its initial activity at 70°C up to 30 min whereas, free formula completely lost its activity at this temperature. Thermodynamics studies showed an enhancement in thermal stability at high temperature for the immobilized xylanase. i.e. At 70°C the t 1/2 and D-value for free formula of enzyme increased from 24 to165 min and from 79.95to 548.23 min, respectively. Moreover, the enzyme stability enhancement for immobilized formula of xylanase was proved with a remarkable increase in enthalpy and free energy. 93% of the immobilized xylanase activity was retained over 6 weeks of storage at -4°C. [ABSTRACT FROM AUTHOR]