Immobilization of alpha-galactosidase on galactose-containing polymeric beads

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dc.contributor.authorOkutucu, Burcu
dc.contributor.authorCelem, Evran Bicak
dc.contributor.authorOnal, Secil
dc.date.accessioned2019-10-27T21:18:37Z
dc.date.available2019-10-27T21:18:37Z
dc.date.issued2010
dc.departmentEge Üniversitesien_US
dc.description.abstractIndustrial application of a-galactosidase requires efficient methods to immobilize the enzyme, yielding a biocatalyst with high activity and stability compared to free enzyme. An alpha-galactosidase from tomato fruit was immobilized on galactose-containing polymeric beads. The immobilized enzyme exhibited an activity of 0.62 U/g of support and activity yield of 46%. The optimum pH and temperature for the activity of both free and immobilized enzymes were found as pH 4.0 and 37 degrees C, respectively. Immobilized alpha-galactosidase was more stable than free enzyme in the range of pH 4.0-6.0 and more than 85% of the initial activity was recovered. The decrease in reaction rate of the immobilized enzyme at temperatures above 37 degrees C was much slower than that of the free counterpart. The immobilized enzyme shows 53% activity at 60 degrees C while free enzyme decreases 33% at the same temperature. The immobilized enzyme retained 50% of its initial activity after 17 cycles of reuse at 37 degrees C. Under same storage conditions, the free enzyme lost about 71% of its initial activity over a period of 7 months, whereas the immobilized enzyme lost about only 47% of its initial activity over the same period. Operational stability of the immobilized enzyme was also studied and the operational half-life (t(1/2) was determined as 6.72 h for p-nitrophenyl alpha-D-galactopyranoside (PNPG) as substrate. The kinetic parameters were determined by using PNPG as substrate. The K-m and V-max values were measured as 1.07 mM and 0.01 U/mg for free enzyme and 0.89 mM and 0.1 U/mg for immobilized enzyme, respectively. The synthesis of the galactose-containing polymeric beads and the enzyme immobilization procedure are very simple and also easy to carry out. (C) 2009 Elsevier Inc. All rights reserved.en_US
dc.identifier.doi10.1016/j.enzmictec.2009.12.005
dc.identifier.endpage205en_US
dc.identifier.issn0141-0229
dc.identifier.issn1879-0909
dc.identifier.issn0141-0229en_US
dc.identifier.issn1879-0909en_US
dc.identifier.issue03.Apren_US
dc.identifier.startpage200en_US
dc.identifier.urihttps://doi.org/10.1016/j.enzmictec.2009.12.005
dc.identifier.urihttps://hdl.handle.net/11454/44014
dc.identifier.volume46en_US
dc.identifier.wosWOS:000274773500007en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.language.isoenen_US
dc.publisherElsevier Science Incen_US
dc.relation.ispartofEnzyme and Microbial Technologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectalpha-Galactosidaseen_US
dc.subjectMolecular imprintingen_US
dc.subjectGalactose-containing polymeric beadsen_US
dc.subjectBioaffinityen_US
dc.subjectImmobilizationen_US
dc.titleImmobilization of alpha-galactosidase on galactose-containing polymeric beadsen_US
dc.typeArticleen_US

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