Bioaffinity immobilization and characterization of ?-galactosidase on aminophenylboronicacid derivatized chitosan and Sepabeads EC-EA

Basit Öğe Kaydı
dc.contributor.authorDemir T.
dc.contributor.authorÖnal S.
dc.date.accessioned2019-10-27T08:02:10Z
dc.date.available2019-10-27T08:02:10Z
dc.date.issued2018
dc.departmentEge Üniversitesien_US
dc.description.abstractEnzyme immobilization with affinity binding which is based on the specific affinity interactions have an important advantage as; high selectivity. In the present study, chitosan and Sepabeads EC-EA were derivatized with aminophenylboronicacid(APBA) for the affinity immobilization of ?-galactosidase. The influence of various process parameters on immobilization of the enzyme is investigated to get high immobilization yields. Under optimized immobilization conditions, the chitosan and Sepabeads EC-EA immobilized enzymes exhibited activity yield of 89.5% and 72%, respectively. The maximum activities were detected at 40 °C for free and Sepabeads EC-EA immobilized enzyme and 55 °C for chitosan immobilized enzyme. The optimum pH was found as pH 5.0 for free and Sepabeads EC-EA immobilized enzyme and pH 5.5 for chitosan immobilized enzyme. Both immobilized enzymes were very stable at temperature ranged from 4 to 55 °C and also in a pH range of 2.6–7.0. The immobilized ?-galactosidases were also used in the hydrolysis of raffinose. The chitosan and Sepabeads EC-EA immobilized enzymes hydrolysed 55% and 42% of raffinose in 32 h at 50 °C, respectively. The obtained results shed light for the useability of these immobilized enzymes in the hydrolysis of raffinose in food industry and make these immobilized enzymes good candidates for their various biotechnological applications. © 2018 Elsevier Ltden_US
dc.description.sponsorship2011 FEN 034en_US
dc.description.sponsorshipThis work has been funded by the Ege University Research Foundation under Project 2011 FEN 034 . We also thank to Dr. Caimi(Resindion S.R.L.) for providing us Sepabeads EC-EA support and for technical help. --en_US
dc.identifier.doi10.1016/j.lwt.2017.12.073
dc.identifier.endpage555en_US
dc.identifier.issn0023-6438
dc.identifier.issn0023-6438en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage547en_US
dc.identifier.urihttps://doi.org/10.1016/j.lwt.2017.12.073
dc.identifier.urihttps://hdl.handle.net/11454/25139
dc.identifier.volume90en_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherAcademic Pressen_US
dc.relation.ispartofLWTen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAffinity immobilizationen_US
dc.subjectAminophenylboronicacid(APBA)en_US
dc.subjectChitosanen_US
dc.subjectSepabeads EC-EAen_US
dc.subject?-galactosidaseen_US
dc.titleBioaffinity immobilization and characterization of ?-galactosidase on aminophenylboronicacid derivatized chitosan and Sepabeads EC-EAen_US
dc.typeArticleen_US

Dosyalar

Koleksiyon

Scopus İndeksli Yayınlar Koleksiyonu