Partial Purification and Characterization of Inulinase Produced from a local isolate of Aspergillus niger J3

Authors

  • Jasim M. Awdaa

DOI:

https://doi.org/10.24126/jobrc.2010.4.2.129

Abstract

Inulinase was produced from local isolate of Aspergillus niger J3. The inulinase was purified by two steps included precipitation by amonium sulphate at (30-80) % sa-turation and gel filtration on sephadex G100. The final purification folds and the yield of the enzyme were 3.15 times and 28.24%, respectively. The purified enzyme has the following characteristics: The optimum pH of the enzyme activity was 5.5. The enzyme was most stable at pH (4.5 - 6). The optimum temperature for its activity was 45c. The enzyme retained its original activity when incubates at (30-55) c for 20 minutes. Mercury chloride inhibited the enzyme completely at concentration of 10mM, cupper sulphate and calisium chloride inhibited the enzyme at concentrations of 85% and 7% respectively. It was revealed that the enzyme had the efficiency to hydrolyze 87% of 5% inulin solution when treated at 45c for 120 min.

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Published

2010-06-01

How to Cite

Awdaa, J. M. . (2010). Partial Purification and Characterization of Inulinase Produced from a local isolate of Aspergillus niger J3. Journal of Biotechnology Research Center, 4(2), 78–85. https://doi.org/10.24126/jobrc.2010.4.2.129

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Section

Research articles