Biochemical characterization of a thermally stable, acidophilic and surfactant-tolerant xylanase from Aspergillus awamori AFE1 and hydrolytic efficiency of its immobilized form

Capital intensiveness of bioconversion of lignocellulosic biomass can be unraveled by producing stable and highly efficient enzyme from phytophilic microbes. The present study revealed biodegradation efficiency of immobilized and free xylanase from Aspergillus awamori AFE1 and the enzyme physicochemical properties. The crude xylanase was subjected to three step purification followed by determination of biochemical properties. The homogenously purified xylanase had an overall 6.86-fold purification and 5.20 % yield coupled with a molecular weight of similar to 48 kDa. Free and immobilized xylanase exhibited optimum activity at (50 degrees C, pH 4) and (70 degrees C, pH 5) respectively while thermal and pH stability for free were achieved at a range of 30-90 degrees C and pH 2-11 respectively. Xylanase was tolerant and enhanced by organic solvents, detergents and inhibitors investigated except ethanol and Cysteine while Mn2+ exceptionally increased xylanase activity and its inhibition by EDTA showed requirement for divalent cations. K-m, 0.15 mM and 1 mM and V-max, 5 x 10(3) mu M/min and 1 x 10(4) mu M/mM were obtained for free and immobilized xylanase. Interestingly, immobilized xylanase showed recycling efficiency of five cycles with higher degradation efficiency over solubilized xylanase. Both free and immobilized xylanase novel characteristics showed suitability for industrial and biotechnological applications.

Automated summary

The study investigates the efficiency and properties of immobilized and free xylanase from Aspergillus awamori AFE1 for biodegradation. The results show that the xylanase exhibits suitable characteristics for industrial and biotechnological applications.