Extraction, Partial Purification and Characterization of Inulinase Produced from Aspergillus niger AN20 by Solid State Fermentation

Abstract

Inulinase produced by Aspergillus niger AN20 was partially purified using two chromatographic techniques, ion exchange chromatography by DEAE-cellulose and gel filtration by Sephadex G-150. The two steps gave specific activity of 810 U/mg proteins, the purification fold was 8.1 and enzymatic yield was 33.5 %. Some biochemical characteristics of the partially purified inulinase were determined and the results revealed that the enzyme have a molecular weight of 42 KDa., optimum pH for  inulinase activity was 4.5, and  the pH of the enzyme stability was the range 4.0-8.0. The maximum activity of purified inulinase activity from A. niger AN20 was determined as 50 ᴼC, while the thermal stability ranges from 20-50 Cᵒ. The aim of this study was the extraction and purification of inulinase produced from Aspergillus niger AN20 by solid state fermentation.