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Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin

Naringinase induced from the fermented broth of marine-derived fungus Aspergillus niger was immobilized into grafted gel beads, to obtain biocatalytically active beads. The support for enzyme immobilization was characterized by ART-FTIR and TGA techniques. TGA revealed a significant improvement in t...

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Detalles Bibliográficos
Autores principales: Awad, Ghada E. A., Abd El Aty, Abeer A., Shehata, Abeer N., Hassan, Mohamed E., Elnashar, Magdy M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4703588/
https://www.ncbi.nlm.nih.gov/pubmed/28330084
http://dx.doi.org/10.1007/s13205-015-0338-x
Descripción
Sumario:Naringinase induced from the fermented broth of marine-derived fungus Aspergillus niger was immobilized into grafted gel beads, to obtain biocatalytically active beads. The support for enzyme immobilization was characterized by ART-FTIR and TGA techniques. TGA revealed a significant improvement in the grafted gel’s thermal stability from 200 to 300 °C. Optimization of the enzyme loading capacity increased gradually by 28-fold from 32 U/g gel to 899 U/g gel beads, retaining 99 % of the enzyme immobilization efficiency and 88 % of the immobilization yield. The immobilization process highly improved the enzyme’s thermal stability from 50 to 70 °C, which is favored in food industries, and reusability test retained 100 % of the immobilized enzyme activity after 20 cycles. These results are very useful on the marketing and industrial levels.