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Erschienen in: Journal of Nanoparticle Research 2/2014

01.02.2014 | Research Paper

Carbodiimide-mediated immobilization of serratiopeptidase on amino-, carboxyl-functionalized magnetic nanoparticles and characterization for target delivery

verfasst von: Sandeep Kumar, Asim K. Jana, Mithu Maiti, Isha Dhamija

Erschienen in: Journal of Nanoparticle Research | Ausgabe 2/2014

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Abstract

A hybrid biomaterial of serratiopeptidase enzyme was prepared with magnetic nanoparticles (MNPs) via carboxyl and amino-functionalization and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) for direct immobilization. The average size of prepared MNPs was found to be 15.05 ± 3.06 nm. Attachment of amino and carboxyl groups was confirmed by Fourier transform infrared spectroscopy. X-ray diffraction confirmed the purity and phase integrity of Fe3O4. The MNPs and enzyme-loaded-MNPs (EMNPs) were of saturation magnetization 58 and 50 emu g−1, respectively. Thermogravimetric analysis of EDC-MNPs and EMNPs showed the presence of organic coating over MNPs. Serratiopeptidase immobilized on amino-functionalized magnetic nanoparticles showed loss of enzyme activity due to crosslinking of enzyme, while serratiopeptidase immobilized on carboxyl-functionalized magnetic nanoparticles was better and gave 115.78 mg protein g−1 MNPs, enzyme loading 168.32 U g−1 MNPs at optimized MNPs-to-enzyme ratio 1.0 mg mg−1. In vitro and in vivo studies showed that EMNPs with magnetic targeting is more effective in drug permeation and reduction in edema than free enzyme.

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Metadaten
Titel
Carbodiimide-mediated immobilization of serratiopeptidase on amino-, carboxyl-functionalized magnetic nanoparticles and characterization for target delivery
verfasst von
Sandeep Kumar
Asim K. Jana
Mithu Maiti
Isha Dhamija
Publikationsdatum
01.02.2014
Verlag
Springer Netherlands
Erschienen in
Journal of Nanoparticle Research / Ausgabe 2/2014
Print ISSN: 1388-0764
Elektronische ISSN: 1572-896X
DOI
https://doi.org/10.1007/s11051-013-2233-x

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