A Positive Effect of Magnetic Field on the Catalytic Activity of Immobilized L-Asparaginase: Evaluation of its Feasibility

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dc.authoridUlu, Ahmet/0000-0002-4447-6233
dc.authoridAteş, Burhan/0000-0001-6080-229X
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.contributor.authorDik, Gamze
dc.contributor.authorUlu, Ahmet
dc.contributor.authorInan, Orhan Orcun
dc.contributor.authorAtalay, Selcuk
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:52:05Z
dc.date.available2024-08-04T20:52:05Z
dc.date.issued2023
dc.departmentİnönü Üniversitesien_US
dc.description.abstractEnzyme immobilization is an attractive strategy to improve enzyme stability, however, the activity significantly reduces after immobilization. To solve this issue, we designed a novel magnetic carrier that both enhanced enzyme activity and improved its stability. For this purpose, the magnetic nanoparticles were synthesized and L-asparaginase was immobilized physically. All materials were structurally and morphologically characterized. Besides, the biochemical properties of the immobilized enzyme were investigated and compared with the free one. Moreover, the activity of the immobilized enzyme was investigated under a weak magnetic field. The optimum pH and optimum temperature of the free and immobilized enzyme were found to be 8.5 and 45 degrees C, 7.5 and 40 degrees C, respectively. Moreover, even after 10 cycles of use, the immobilized enzyme retained 54% of its initial activity. K-m for free and the immobilized enzyme was found to be 10.37 +/- 0.5, and 7.06 +/- 2.99 mM, respectively, and V-max was found to be 138.88 +/- 2.64, and 121.95 +/- 1.07 molimin, respectively. Most importantly, the activity increased approximately 3.2-fold and 4.3-fold at 10 Hz and 20 mT, respectively. Overall, the results suggested that, if the activity of the immobilized enzyme is very low, applying a weak magnetic field may be necessary to enhance the enzyme reaction. [GRAPHICS] .en_US
dc.description.sponsorshipScientific Research Projects Unit of Inonu University [FYL-2019-1865]; National Boron Research Instituteen_US
dc.description.sponsorshipThe authors are grateful to the Scientific Research Projects Unit of Inonu University (project number FYL-2019-1865) and to the National Boron Research Institute to recognize the financial support. This study was derived from the master thesis presented by Gamze Dik (2021-685201).en_US
dc.identifier.doi10.1007/s10562-022-04075-3
dc.identifier.endpage1264en_US
dc.identifier.issn1011-372X
dc.identifier.issn1572-879X
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-85132694481en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1250en_US
dc.identifier.urihttps://doi.org/10.1007/s10562-022-04075-3
dc.identifier.urihttps://hdl.handle.net/11616/100740
dc.identifier.volume153en_US
dc.identifier.wosWOS:000815438800002en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofCatalysis Lettersen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectMagnetic nanoparticlesen_US
dc.subjectBoronic aciden_US
dc.subjectEnzyme immobilizationen_US
dc.subjectL-asparaginaseen_US
dc.subjectMagnetic fielden_US
dc.subjectEnhanced activityen_US
dc.titleA Positive Effect of Magnetic Field on the Catalytic Activity of Immobilized L-Asparaginase: Evaluation of its Feasibilityen_US
dc.typeArticleen_US

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