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Maltose Functionalized Magnetic Core/Shell Fe3O4@Au Nanoparticles for An Efficient L-Asparaginase Immobilization

dc.authorid 0000-0003-2656-4464
dc.authorid 0000-0003-2656-4464
dc.contributor.author Tarhan, Tuba
dc.contributor.author Ulu, Ahmet
dc.contributor.author Sariçam, Melike
dc.contributor.author Çulha, Mustafa
dc.contributor.author Ates, Burhan
dc.contributor.other Department of Medical Services and Techniques / Tıbbi Hizmetler ve Teknikleri Bölümü
dc.date.accessioned 2020-01-02T19:16:44Z
dc.date.available 2020-01-02T19:16:44Z
dc.date.issued 2020
dc.department MAÜ, Meslek Yüksekokulları, Sağlık Hizmetleri Meslek Yüksekokulu, Tıbbi Hizmetler ve Teknikler Bölümü en_US
dc.description.abstract In this study, maltose-functionalized magnetic core/shell nanoparticles (Fe3O4@Au NPs) as a promising carrier matrix for a simple and effective immobilization of L-asparaginase (L ASNase) were prepared and characterized using imaging techniques including atomic force microscopy (AFM) and transmission electron microscopy (TEM), and vibrating sample magnetometry (VSM). The results indicate that the NPs are monodispersed with an average diameter of 10 nm and magnetization of 9.0 emu g-1. Under the optimal conditions, 77.2 ± 2.3% of the total L-ASNase was immobilized. It was found that the acid-base tolerance and thermal stability of immobilized L-ASNase were significantly improved in comparison to the free form of the enzyme in solution. For instance, while only 10% of the immobilized enzyme was lost its activity, the free form was lost its activity more than 50% after 3 h incubation at 55 oC. After 13 times recycling, the immobilized L-ASNase retained about 50% of its initial activity. Moreover, the free and immobilized L-ASNase maintained their initial activities about 25 and 64% after 28 days storage at 25 °C, respectively. Km value of immobilized L-ASNase decreased to 1.59 from 2.95 mM as an indication of increased enzyme affinity for the substrate. The results of this study suggest that the maltose-coated magnetic nanoparticles are excellent nanovehicles to carry enzymes for a range of industrial applications. en_US
dc.description.citation Tarhan T, Ulu A, Sariçam M, Çulha M, Ates B. Maltose functionalized magnetic core/shell Fe3O4@Au nanoparticles for an efficient l-asparaginase immobilization. Int J Biol Macromol. 2020 Jan 1;142:443-451. doi: 10.1016/j.ijbiomac.2019.09.116. Epub 2019 Oct 5. PMID: 31593716. en_US
dc.identifier.uri https://hdl.handle.net/20.500.12514/2097
dc.identifier.uri https://pubmed.ncbi.nlm.nih.gov/31593716/
dc.identifier.uri https://doi.org/10.1016/j.ijbiomac.2019.09.116
dc.indekslendigikaynak Web of Science en_US
dc.indekslendigikaynak Scopus en_US
dc.indekslendigikaynak PubMed en_US
dc.language.iso en en_US
dc.publisher International Journal of Biological Macromolecules en_US
dc.relation.publicationcategory Makale - Uluslararası - Editör Denetimli Dergi en_US
dc.rights info:eu-repo/semantics/closedAccess en_US
dc.subject Magnetic Core/Shell Nanoparticles, L-Asparaginase, Immobilization, Maltose en_US
dc.title Maltose Functionalized Magnetic Core/Shell Fe3O4@Au Nanoparticles for An Efficient L-Asparaginase Immobilization en_US
dc.type Article en_US
dspace.entity.type Publication
relation.isAuthorOfPublication e0108707-5da9-4603-92e8-4eeb919ff91f
relation.isAuthorOfPublication.latestForDiscovery e0108707-5da9-4603-92e8-4eeb919ff91f
relation.isOrgUnitOfPublication 256d1c0a-4c75-476b-b468-80c6b6a899f2
relation.isOrgUnitOfPublication.latestForDiscovery 256d1c0a-4c75-476b-b468-80c6b6a899f2

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