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dc.contributor.authorAwad, G.
dc.contributor.authorAbd El Aty, A.
dc.contributor.authorShehata, A.
dc.contributor.authorHassan, M.
dc.contributor.authorElnashar, Magdy
dc.date.accessioned2017-01-30T10:26:44Z
dc.date.available2017-01-30T10:26:44Z
dc.date.created2016-03-16T19:30:17Z
dc.date.issued2016
dc.identifier.citationAwad, G. and Abd El Aty, A. and Shehata, A. and Hassan, M. and Elnashar, M. 2016. Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin. 3 Biotech. 6: Article ID 14.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/2854
dc.identifier.doi10.1007/s13205-015-0338-x
dc.description.abstract

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.

dc.publisherSpringer
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.titleCovalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin
dc.typeJournal Article
dcterms.source.volume6
dcterms.source.startPage1
dcterms.source.endPage10
dcterms.source.issn2190-5738
dcterms.source.title3 Biotech
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusOpen access


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