Extraction, partial purification and characterization of inulinase produced from Aspergillus Niger AN20 by solid state fermentation

الملخص EN

Inulinase produced by Aspergillus niger AN20 was partially purified using two chroma-tographic techniques, ion exchange chromatography by DEAE-cellulose and gel filtration by Se-phadex 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 in-ulinase 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.