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

  • Ghazi M. Aziz1, Zainab W. Abdulameer1, Ali J. R. AL-Sa'ady1

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.

 

Published
2019-03-03