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Immobilization of bovine catalase onto magnetic nanoparticles.
MedLine Citation:
PMID:  23876136     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
The scope of this study is to achieve carrier-bound immobilization of catalase onto magnetic particles (Fe3O4 and Fe2O3NiO2 · H2O) to specify the optimum conditions of immobilization. Removal of H2O2 and the properties of immobilized sets were also investigated. To that end, adsorption and then cross-linking methods onto magnetic particles were performed. The optimum immobilization conditions were found for catalase: immobilization time (15 min for Fe3O4; 10 min for Fe2O3NiO2 · H2O), the initial enzyme concentration (1 mg/mL), amount of magnetic particles (25 mg), and glutaraldehyde concentration (3%). The activity reaction conditions (optimum temperature, optimum pH, pH stability, thermal stability, operational stability, and reusability) were characterized. Also kinetic parameters were calculated by Lineweaver-Burk plots. The optimum pH values were found to be 7.0, 7.0, and 8.0 for free enzyme, Fe3O4-immobilized catalases, and Fe2O3NiO2 · H2O-immobilized catalases, respectively. All immobilized catalase systems displayed the optimum temperature between 25 and 35°C. Reusability studies showed that Fe3O4-immobilized catalase can be used 11 times with 50% loss in original activity, while Fe2O3NiO2 · H2O-immobilized catalase lost 67% of activity after the same number of uses. Furthermore, immobilized catalase systems exhibited improved thermal and pH stability. The results transparently indicate that it is possible to have binding between enzyme and magnetic nanoparticles.
Authors:
Yasemin İspirli Doğaç; Mustafa Teke
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Preparative biochemistry & biotechnology     Volume:  43     ISSN:  1532-2297     ISO Abbreviation:  Prep. Biochem. Biotechnol.     Publication Date:  2013 Nov 
Date Detail:
Created Date:  2013-07-23     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9607037     Medline TA:  Prep Biochem Biotechnol     Country:  England    
Other Details:
Languages:  eng     Pagination:  750-65     Citation Subset:  IM    
Affiliation:
a Chemistry Department, Faculty of Science , Muğla Sıtkı Koçman University , Muğla , Turkey.
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