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Evaluation of Designed Immobilized Catalytic Systems: Activity Enhancement of Lipase B from Candida antarctica

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dc.contributor Háskóli Íslands
dc.contributor University of Iceland
dc.contributor.author Siódmiak, Tomasz
dc.contributor.author Haraldsson, Guðmundur G.
dc.contributor.author Dulęba, Jacek
dc.contributor.author Ziegler-Borowska, Marta
dc.contributor.author Siódmiak, Joanna
dc.contributor.author Marszałł, Michał Piotr
dc.date.accessioned 2020-11-30T09:49:40Z
dc.date.available 2020-11-30T09:49:40Z
dc.date.issued 2020-08-04
dc.identifier.citation Siódmiak, T.; G. Haraldsson, G.; Dulęba, J.; Ziegler-Borowska, M.; Siódmiak, J.; Marszałł, M.P. Evaluation of Designed Immobilized Catalytic Systems: Activity Enhancement of Lipase B from Candida antarctica. Catalysts 2020, 10, 876.
dc.identifier.issn 2073-4344
dc.identifier.uri https://hdl.handle.net/20.500.11815/2251
dc.description Publisher's version (útgefin grein)
dc.description.abstract Immobilized enzymatic catalysts are widely used in the chemical and pharmaceutical industries. As Candida antarctica lipase B (CALB) is one of the more commonly used biocatalysts, we attempted to design an optimal lipase-catalytic system. In order to do that, we investigated the enantioselectivity and lipolytic activity of CALB immobilized on 12 different supports. Immobilization of lipase on IB-D152 allowed us to achieve hyperactivation (178%) in lipolytic activity tests. Moreover, the conversion in enantioselective esterification increased 43-fold, when proceeding with lipase-immobilized on IB-S861. The immobilized form exhibited a constant high catalytic activity in the temperature range of 25 to 55°C. Additionally, the lipase immobilized on IBD152 exhibited a higher lipolytic activity in the pH range of 6 to 9 compared with the native form. Interestingly, our investigations showed that IB-S500 and IB-S60S offered a possibility of application in catalysis in both organic and aqueous solvents. A significant link between the reaction media, the substrates, the supports and the lipase was confirmed. In our enzymatic investigations, highperformance liquid chromatography (HPLC) and the titrimetric method, as well as the Bradford method were employed.
dc.description.sponsorship This work was supported by the National Science Centre Poland grant DEC-2013/09/N/NZ7/03557.
dc.format.extent 876
dc.language.iso en
dc.publisher MDPI AG
dc.relation.ispartofseries Catalysts;10(8)
dc.rights info:eu-repo/semantics/openAccess
dc.subject Biocatalysis
dc.subject Candida antarctica lipase B
dc.subject Enantioselectivity
dc.subject Immobeads
dc.subject Immobilization
dc.subject Lipolytic activity
dc.subject Reaction medium
dc.subject Supports
dc.subject Lyfjaefnafræði
dc.title Evaluation of Designed Immobilized Catalytic Systems: Activity Enhancement of Lipase B from Candida antarctica
dc.type info:eu-repo/semantics/article
dcterms.license This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited
dc.description.version Peer Reviewed
dc.identifier.journal Catalysts
dc.identifier.doi 10.3390/catal10080876
dc.relation.url https://www.mdpi.com/2073-4344/10/8/876/pdf
dc.contributor.department Raunvísindastofnun (HÍ)
dc.contributor.department Science Institute (UI)
dc.contributor.school Verkfræði- og náttúruvísindasvið (HÍ)
dc.contributor.school School of Engineering and Natural Sciences (UI)

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