Different spacer-arm attached magnetic nanoparticles for covalent immobilization of Jack bean urease

MakaleAçık Erişim

Özet

Objectives: This study aims the covalent immobilization of Jack bean urease on Fe3O4 magnetic nanoparticles via glutaraldehyde (urease@MNPs-Si-Glu) and epichlorohydrin (urease@MNPs-ECH) spacer arms. Methods: The optimum pH and temperature, thermal, storage and reuse stability of free and immobilized urease preparations were investigated. Thermodynamics characterizations of free and immobilized urease preparations were also studied. Results: The free urease and both immobilized urease preparations showed maximal catalytic activity at pH 7.5. The free urease had a maximal catalytic activity at 50 °C, while the both immobilized urease preparations exhibited their maximal catalytic activities at 70 °C. The urease@MNPs-Si-Glu and urease@MNP-ECH showed 2.7- and 1.9-fold higher thermal stability than the free urease at 60 °C, respectively. The free urease remained 30% of their initial activity at 4 °C, while urease@MNPs-Si-Glu and urease@MNPs-ECH retained 72 and 60% of their initial activities at the same conditions. The urease@MNPs-Si-Glu and urease@MNPs-ECH preserved 53 and 52% of their initial activities, respectively for urea hydrolysis after 20 reuses. Conclusions: The urease@MNPs-Si-Glu and urease@MNPsECH may find a potential application area in urea hydrolysis.

Anahtar Kelimeler

RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/gumushane/12834Resmi atıflarda kullanılan kalıcı adres
DOI
https://doi.org/10.1515/tjb-2021-0264Yayıncı resmi DOI adresi
Tam Kayıt
AlanDeğerDil
dc.contributor.authorGulesci, Nuri
dc.contributor.authorYucebilgic, Guzide
dc.contributor.authorYildirim, Deniz
dc.date.accessioned2026-10-22T10:20:35.851795032Z
dc.date.available2026-10-22T10:20:35.851795032Z
dc.date.issued2022
dc.description.abstractObjectives: This study aims the covalent immobilization of Jack bean urease on Fe3O4 magnetic nanoparticles via glutaraldehyde (urease@MNPs-Si-Glu) and epichlorohydrin (urease@MNPs-ECH) spacer arms. Methods: The optimum pH and temperature, thermal, storage and reuse stability of free and immobilized urease preparations were investigated. Thermodynamics characterizations of free and immobilized urease preparations were also studied. Results: The free urease and both immobilized urease preparations showed maximal catalytic activity at pH 7.5. The free urease had a maximal catalytic activity at 50 °C, while the both immobilized urease preparations exhibited their maximal catalytic activities at 70 °C. The urease@MNPs-Si-Glu and urease@MNP-ECH showed 2.7- and 1.9-fold higher thermal stability than the free urease at 60 °C, respectively. The free urease remained 30% of their initial activity at 4 °C, while urease@MNPs-Si-Glu and urease@MNPs-ECH retained 72 and 60% of their initial activities at the same conditions. The urease@MNPs-Si-Glu and urease@MNPs-ECH preserved 53 and 52% of their initial activities, respectively for urea hydrolysis after 20 reuses. Conclusions: The urease@MNPs-Si-Glu and urease@MNPsECH may find a potential application area in urea hydrolysis.
dc.description.sponsorshipÇukurova Üniversitesi, CU
dc.identifier.doi10.1515/tjb-2021-0264
dc.identifier.eissn1303-829X
dc.identifier.endpage509
dc.identifier.issn0250-4685
dc.identifier.issue4
dc.identifier.scopus2-s2.0-85146380974
dc.identifier.startpage501
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/gumushane/12834
dc.identifier.volume47
dc.identifier.wosWOS:000778319700001
dc.language.isoen
dc.publisherDe Gruyter Open Ltd
dc.relation.ispartofTurkish Journal of Biochemistry
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectepichlorohydrin
dc.subjectglutaraldehyde
dc.subjectimmobilization
dc.subjectmagnetic nanoparticles
dc.subjecturease
dc.subject.classificationBiochemistry & Molecular Biology
dc.subject.otherepichlorohydrin
dc.subject.otherglutaraldehyde
dc.subject.othermagnetic nanoparticle
dc.subject.otherurease
dc.subject.otherxylan endo 1,3 beta xylosidase
dc.subject.otherArticle
dc.subject.otherdrug synthesis
dc.subject.otherenzyme activity
dc.subject.othergenomic instability
dc.subject.otherimmobilization
dc.subject.otherinfrared spectroscopy
dc.subject.otherpH
dc.subject.otherscanning electron microscopy
dc.subject.othertemperature
dc.subject.otherthermodynamics
dc.subject.otherthermogravimetry
dc.subject.otherthermostability
dc.titleDifferent spacer-arm attached magnetic nanoparticles for covalent immobilization of Jack bean urease
dc.typeArticle
dspace.entity.typePublication
rdl.citation.openalex3
rdl.citation.scopus3
rdl.citation.trdizin0
rdl.citation.wos2
rdl.oa.statusgold
rdl.oa.urlhttps://www.degruyter.com/document/doi/10.1515/tjb-2021-0264/pdf
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.source.indexTRDIZIN
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)