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Mater Sci Eng C Mater Biol Appl ; 38: 46-54, 2014 May 01.
Artículo en Inglés | MEDLINE | ID: mdl-24656351

RESUMEN

In the present study, different proteins, namely, bovine serum albumin (BSA), glucose oxidase (GOx) and the laboratory purified YqeH were immobilized in the phenolic resin precursor-based multi-scale web of activated carbon microfibers (ACFs) and carbon nanofibers (CNFs). These biomolecules are characteristically different from each other, having different structure, number of parent amino acid molecules and isoelectric point. CNF was grown on ACF substrate by chemical vapor deposition, using Ni nanoparticles (Nps) as the catalyst. The ultra-sonication of the CNFs was carried out in acidic medium to remove Ni Nps from the tip of the CNFs to provide additional active sites for adsorption. The prepared material was directly used as an adsorbent for proteins, without requiring any additional treatment. Several analytical techniques were used to characterize the prepared materials, including scanning electron microscopy, Fourier transform infrared spectroscopy, BET surface area, pore-size distribution, and UV-vis spectroscopy. The adsorption capacities of prepared ACFs/CNFs in this study were determined to be approximately 191, 39 and 70 mg/g for BSA, GOx and YqeH, respectively, revealing that the carbon micro-nanofibers forming synthesized multi-scale web are efficient materials for the immobilization of protein molecules.


Asunto(s)
Carbono/química , Proteínas Inmovilizadas/metabolismo , Nanofibras/química , Adsorción , Animales , Bovinos , Carbón Orgánico/química , Glucosa Oxidasa/metabolismo , Cinética , Nanofibras/ultraestructura , Níquel/química , Nitrógeno/química , Albúmina Sérica Bovina/metabolismo , Sonicación , Espectroscopía Infrarroja por Transformada de Fourier , Espectrometría Raman , Propiedades de Superficie , Temperatura
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