Different spacer-arm attached magnetic nanoparticles for covalent immobilization of Jack bean urease
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
- Scopus
- 3
- WoS
- 2
- OpenAlex
- 3
- TR Dizin
- 0
Tam Kayıt
| Alan | Değer | Dil |
|---|---|---|
| dc.contributor.author | Gulesci, Nuri | |
| dc.contributor.author | Yucebilgic, Guzide | |
| dc.contributor.author | Yildirim, Deniz | |
| dc.date.accessioned | 2026-10-22T10:20:35.851795032Z | |
| dc.date.available | 2026-10-22T10:20:35.851795032Z | |
| dc.date.issued | 2022 | |
| dc.description.abstract | 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. | |
| dc.description.sponsorship | Çukurova Üniversitesi, CU | |
| dc.identifier.doi | 10.1515/tjb-2021-0264 | |
| dc.identifier.eissn | 1303-829X | |
| dc.identifier.endpage | 509 | |
| dc.identifier.issn | 0250-4685 | |
| dc.identifier.issue | 4 | |
| dc.identifier.scopus | 2-s2.0-85146380974 | |
| dc.identifier.startpage | 501 | |
| dc.identifier.uri | https://rdlopen.rawdatalibrary.net/r/gumushane/12834 | |
| dc.identifier.volume | 47 | |
| dc.identifier.wos | WOS:000778319700001 | |
| dc.language.iso | en | |
| dc.publisher | De Gruyter Open Ltd | |
| dc.relation.ispartof | Turkish Journal of Biochemistry | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.subject | epichlorohydrin | |
| dc.subject | glutaraldehyde | |
| dc.subject | immobilization | |
| dc.subject | magnetic nanoparticles | |
| dc.subject | urease | |
| dc.subject.classification | Biochemistry & Molecular Biology | |
| dc.subject.other | epichlorohydrin | |
| dc.subject.other | glutaraldehyde | |
| dc.subject.other | magnetic nanoparticle | |
| dc.subject.other | urease | |
| dc.subject.other | xylan endo 1,3 beta xylosidase | |
| dc.subject.other | Article | |
| dc.subject.other | drug synthesis | |
| dc.subject.other | enzyme activity | |
| dc.subject.other | genomic instability | |
| dc.subject.other | immobilization | |
| dc.subject.other | infrared spectroscopy | |
| dc.subject.other | pH | |
| dc.subject.other | scanning electron microscopy | |
| dc.subject.other | temperature | |
| dc.subject.other | thermodynamics | |
| dc.subject.other | thermogravimetry | |
| dc.subject.other | thermostability | |
| dc.title | Different spacer-arm attached magnetic nanoparticles for covalent immobilization of Jack bean urease | |
| dc.type | Article | |
| rdl.citation.openalex | 3 | |
| rdl.citation.scopus | 3 | |
| rdl.citation.trdizin | 0 | |
| rdl.citation.wos | 2 | |
| rdl.oa.status | gold | |
| rdl.oa.url | https://www.degruyter.com/document/doi/10.1515/tjb-2021-0264/pdf | |
| rdl.scopus.quartile | Q4 | |
| rdl.source.index | SCOPUS | |
| rdl.source.index | WOS | |
| rdl.source.index | TRDIZIN | |
| rdl.wos.index | Science Citation Index Expanded (SCI-EXPANDED) |

