Immobilization of β-galactosidase onto magnetic poly(GMA–MMA) beads for hydrolysis of lactose in bed reactor
dc.contributor.author | Bayramogğu, Gülay | |
dc.contributor.author | Tunali, Yagmur | |
dc.contributor.author | Arica, M. Yakup | |
dc.date.accessioned | 2020-06-25T17:43:43Z | |
dc.date.available | 2020-06-25T17:43:43Z | |
dc.date.issued | 2007 | |
dc.description.abstract | In the present study, novel magnetic beads were prepared from glycidylmethacrylate and methylmethacrylate via suspension polymerization in the presence of a cross-linker (i.e. ethylenedimethylmethacrylate). The magnetic poly(GMA-MMA) beads were characterized with scanning electron microscope, FT-IR and ESR spectrophotometers. The reactive character of the epoxy groups allowed the attachment of the amino groups. The aminated magnetic beads were used for the covalent immobilization of beta-galactosidase via glutaric dialdehyde activation. The maximum amount of immobilized beta-galactosidase on the magnetic poly(GMA-MMA) beads was 9.87 mg/g support. The values of Michaelis constants K-m for immobilized beta-galactosidase was significant larger, indicating decreased affinity by the enzyme for its substrate, whereas V-max values were smaller for the immobilized beta P-galactosidase. However, the beta-galactosidase immobilized on the magnetic poly(GMA-MMA) beads resulted in an increase in enzyme stability with time. Optimum operational temperature for immobilized enzyme was 5 degrees C higher than that of the free enzyme and was significantly broader. Finally, a bed reactor with P-galactosidase immobilized was used for hydrolysis of lactose. The enzyme reactor operated continuously at 35 degrees C for 60 h and the immobilized enzyme lost about 12% of its initial activity after this period. (C) 2006 Elsevier B.V. All rights reserved. | en_US |
dc.identifier.citation | closedAccess | en_US |
dc.identifier.doi | 10.1016/j.catcom.2006.10.029 | |
dc.identifier.endpage | 1101 | en_US |
dc.identifier.issn | 1566-7367 | |
dc.identifier.issn | 1873-3905 | |
dc.identifier.issue | 7 | en_US |
dc.identifier.scopus | 2-s2.0-34248232512 | |
dc.identifier.scopusquality | Q2 | |
dc.identifier.startpage | 1094 | en_US |
dc.identifier.uri | https://doi.org10.1016/j.catcom.2006.10.029 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12587/3867 | |
dc.identifier.volume | 8 | en_US |
dc.identifier.wos | WOS:000247133800024 | |
dc.identifier.wosquality | Q2 | |
dc.indekslendigikaynak | Web of Science | |
dc.indekslendigikaynak | Scopus | |
dc.language.iso | en | |
dc.publisher | Elsevier | en_US |
dc.relation.ispartof | Catalysis Communications | |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | magnetic beads | en_US |
dc.subject | enzyme immobilization | en_US |
dc.subject | beta-galactosidase | en_US |
dc.subject | kinetic parameters | en_US |
dc.subject | enzyme reactor | en_US |
dc.title | Immobilization of β-galactosidase onto magnetic poly(GMA–MMA) beads for hydrolysis of lactose in bed reactor | en_US |
dc.type | Article |
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