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A facile preparation of immobilized naringinase on polyethyleneimine-modified Fe(3)O(4) magnetic nanomaterials with high activity
Polyethyleneimine-modified Fe(3)O(4) nanoparticles (Fe(3)O(4)-PEI) were synthesized by the one-step co-precipitation method, and the resulting material was used to immobilize naringinase from the fermentation broth of Aspergillus niger FFCC uv-11. The immobilized naringinase activity could reach up...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8698058/ https://www.ncbi.nlm.nih.gov/pubmed/35424008 http://dx.doi.org/10.1039/d1ra01449h |
Sumario: | Polyethyleneimine-modified Fe(3)O(4) nanoparticles (Fe(3)O(4)-PEI) were synthesized by the one-step co-precipitation method, and the resulting material was used to immobilize naringinase from the fermentation broth of Aspergillus niger FFCC uv-11. The immobilized naringinase activity could reach up to 690.74 U per g-support at the conditions of initial naringinase activity of 406.25 U mL(−1), immobilization time of 4 h, glutaraldehyde concentration of 40% (w/v), immobilization temperature of 35 °C, and pH value of 5.5, with naringinase-carrying rate and naringinase activity recovery of 92.93% and 20.89%, respectively. In addition, the immobilized naringinase exhibited good pH and temperature stability in a pH range of 3.5–6.0 and temperature range of 40–70 °C, and the optimal reaction pH and reaction temperature were optimized as 5.5 and 60 °C, respectively. Besides, the immobilized naringinase could maintain 60.58% of the original activity after 10 reuse cycles, indicating that the immobilized naringinase had good reusability. Furthermore, the immobilized naringinase also performed excellent storage stability, 87.52% of enzyme activity still remained as stored at 4 °C for one month. In conclusion, the Fe(3)O(4)-PEI could be considered as a promising support for naringinase immobilization, with the advantages of high enzyme activity loading, good reusability, storage stability and rapid recovery. |
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