Optimization of thermostable inulinase production from Aspergillus niger NRRL 3122, purification, and characterization | ||
| Research Journal of Applied Biotechnology | ||
| Article 2, Volume 7, Issue 1, June 2021, Pages 15-29 PDF (374.63 K) | ||
| Document Type: Original Article | ||
| DOI: 10.21608/rjab.2021.303287 | ||
| Authors | ||
| Ahmed Bisher; Mahmoud Alsaman; Asmaa Abdelaa* ; Hoda Mahrous | ||
| Department of Industrial Biotechnology, Genetic Engineering and Biotechnology Research Institute, University of Sadat City, Sadat City, Egypt | ||
| Abstract | ||
| Inulinase is a versatile glycoside hydrolase enzyme that targets the -2, 1 linkage of fructopolymers. The objective of the study was to produce inulinase using a low-cost carbon source from Aspergillus niger NRRL 3122, which was successful in producing a high titer of inulinase on agave. The Plackett-Burman design and Box-Behnken design were used to optimize the production of inulinase, which resulted in a high inulinase titer of 2170.22 U/ml, which is 2.83 times higher than the screening. The optimal levels of agave, NaNO3, and KCl were found to be 10 g/L, 4 g/L, and 0.3 g/L, respectively. The molecular weight of the enzyme was around 50 KDa. The enzyme showed maximum performance at 50°C and pH 6.0, and temperature stability up to 70°C, while pH stability was observed between 4-6. The pure inulinase could only hydrolyze inulin and sucrose, and not cellobiose and soluble starches. The Km and Vmax values for inulin were found to be 0.76 mg/mL and 100,000 U/mg, respectively. | ||
| Keywords | ||
| Aspergillus niger NRRL 3122; inulinase; agave; Plackett-Burman, Box-Behnken purification, characterization | ||
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