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...
| Main Authors: | , , , , |
|---|---|
| Format: | Journal Article |
| Published: |
Springer
2016
|
| Online Access: | http://hdl.handle.net/20.500.11937/2854 |
| _version_ | 1848744067775594496 |
|---|---|
| author | Awad, G. Abd El Aty, A. Shehata, A. Hassan, M. Elnashar, Magdy |
| author_facet | Awad, G. Abd El Aty, A. Shehata, A. Hassan, M. Elnashar, Magdy |
| author_sort | Awad, G. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T05:55:34Z |
| format | Journal Article |
| id | curtin-20.500.11937-2854 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T05:55:34Z |
| publishDate | 2016 |
| publisher | Springer |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-28542018-04-19T07:10:12Z Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin Awad, G. Abd El Aty, A. Shehata, A. Hassan, M. Elnashar, Magdy 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. 2016 Journal Article http://hdl.handle.net/20.500.11937/2854 10.1007/s13205-015-0338-x http://creativecommons.org/licenses/by/4.0/ Springer fulltext |
| spellingShingle | Awad, G. Abd El Aty, A. Shehata, A. Hassan, M. Elnashar, Magdy Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin |
| title | Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin |
| title_full | Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin |
| title_fullStr | Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin |
| title_full_unstemmed | Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin |
| title_short | Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin |
| title_sort | covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin |
| url | http://hdl.handle.net/20.500.11937/2854 |