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Urease-Dextran complexes with enhanced enzymatic activity and stability

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dc.contributor.authorYapaoz, Melda Altikatoglu
dc.contributor.authorDestanoglu, Azra
dc.date.accessioned2026-06-27T14:10:35Z
dc.date.issued2017
dc.description.abstractIn this study, the urease-dextran non-covalent complexes in various molar ratios were synthesized and compared to the free enzyme in terms of pH, temperature, thermal and storage stabilities. Especially, the complex with a molar ratio of n(U)/n(DA) = 40/1 showed highest thermal stability and had ca. 1.4-fold at 25 degrees C and 2.5-fold at 80 degrees C higher activity than the free enzyme. The complex showed a high catalytic activity in organic solvent. In addition, the thermal and storage stabilities of urease were improved greatly as dextran complex, which has advantages for usage in practice.en
dc.description.sponsorshipYildiz Technical University research fund [2016-01-02-KAP02]
dc.description.sponsorshipTUBITAK [114Z138]
dc.description.urihttps://doi.org/10.1080/07328303.2017.1403614
dc.identifier.doi10.1080/07328303.2017.1403614
dc.identifier.eissn1532-2327
dc.identifier.endpage335
dc.identifier.issn0732-8303
dc.identifier.issue8-9
dc.identifier.startpage325
dc.identifier.urihttps://hdl.handle.net/20.500.14981/57579
dc.identifier.volume36
dc.identifier.wos000419969900004
dc.language.isoeng
dc.publisherTAYLOR & FRANCIS INC
dc.relation.ispartofJOURNAL OF CARBOHYDRATE CHEMISTRY
dc.subjectstabilization
dc.subjecturease
dc.subjectdextran
dc.subjectcomplex
dc.subjectORGANIC-SOLVENTS
dc.subjectGLUCOSE-OXIDASE
dc.subjectIMMOBILIZATION
dc.subjectENZYMES
dc.subjectTEMPERATURE
dc.subjectCHITOSAN
dc.subjectPH
dc.subjectCOACERVATION
dc.subjectMICROENCAPSULATION
dc.subjectPOLYSACCHARIDES
dc.subjectBiochemistry & Molecular Biology
dc.subjectChemistry
dc.titleUrease-Dextran complexes with enhanced enzymatic activity and stability
dc.typeArticle
dspace.entity.typePublication
local.import.sourceWOS

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