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dc.creatorKaličanin, Nevena
dc.creatorKovačević, Gordana
dc.creatorSpasojević, Milica
dc.creatorProdanović, Olivera
dc.creatorJovanović-Šanta, Suzana
dc.creatorŠkorić, Dušan
dc.creatorOpsenica, Dejan
dc.creatorProdanović, Radivoje
dc.date.accessioned2023-01-09T18:10:21Z
dc.date.available2023-08-13
dc.date.issued2022
dc.identifier.issn1359-5113
dc.identifier.urihttps://cer.ihtm.bg.ac.rs/handle/123456789/5545
dc.description.abstractThe aim of this research was to improve the operational stability and enable the reusability of ω-transaminase for synthesis of new enantiopure chiral amines of steroids. Dihydrotestosterone was used to optimize the synthetic procedure of corresponding amino-steroid on a larger scale. The obtained product 3α-amino-5α-androstan-17β-ol was isolated and characterized. The enzyme was immobilized on a methacrylate-based carrier, giving the specific activity of 1.84 U/g of dry polymer. Higher residual activity of the immobilized enzyme in comparison to the soluble form (100 % versus 35%) after 24 h incubation in 35 % dimethylformamide (DMF) was obtained. The soluble enzyme retained 19 % of the initial activity after 2 h incubation in 35 % DMF at 70 °C, while the activity of the immobilized enzyme decreased only to 75 %. Immobilized retained 85 % of initial activity after ten consecutive cycles of 3α-amino-5α-androstan-17β-ol synthesis. We have tested the specificity of the ArRMut11 variant, further increased its stability by immobilization, and used it in several cycles for the synthesis of 3α-amino-5α-androstan-17β-ol. We showed that the enzyme previously evolved for higher stability as the immobilized variant showed more increased stability and high reusability that can more effectively be applied for the biosynthesis of amino steroids.sr
dc.language.isoensr
dc.publisherElseviersr
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200288/RS//sr
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200053/RS//sr
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200168/RS//sr
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200026/RS//sr
dc.relation.isversionofhttps://cer.ihtm.bg.ac.rs/handle/123456789/5370
dc.relation.isversionofhttps://doi.org/10.1016/j.procbio.2022.08.016
dc.rightsembargoedAccesssr
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceProcess Biochemistrysr
dc.subjectBiocatalystssr
dc.subjectDihydrotestosteronesr
dc.subjectImmobilizationsr
dc.subjectMacroporoussr
dc.subjectSteroidsr
dc.titleImmobilization of ArRMut11 omega-transaminase for increased operational stability and reusability in the synthesis of 3α-amino-5α-androstan-17β-olsr
dc.typearticlesr
dc.rights.licenseBY-NC-NDsr
dc.citation.volume121
dc.citation.spage674
dc.citation.epage680
dc.citation.rankM21~
dc.description.otherThis is the peer-reviewed version of the article: Nevena Kaličanin, Gordana Kovačević, Milica Spasojević, Olivera Prodanović, Suzana Jovanović-Šanta, Dušan Škorić, Dejan Opsenica and Radivoje Prodanović, Immobilization of ArRMut11 omegatransaminase for increased operational stability and reusability in the synthesis of 3α-amino-5α-androstan-17β-ol, Process Biochemistry, (2022) 121, 674-680 [doi:https://doi.org/10.1016/j.procbio.2022.08.016]
dc.description.otherPublished version: [https://cer.ihtm.bg.ac.rs/handle/123456789/5370]
dc.identifier.doi10.1016/j.procbio.2022.08.016
dc.identifier.fulltexthttp://cer.ihtm.bg.ac.rs/bitstream/id/23364/1-s2.0-S1359511322003002-main.pdf
dc.identifier.scopus2-s2.0-85136125602
dc.type.versionacceptedVersionsr


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