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Enzyme Microb Technol ; 63: 50-7, 2014 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-25039060

RESUMO

A novel magnetic Fe3O4 nanoparticles (MNPs) coupled with agarose (AMNPs) was synthesized using co-precipitation via alkaline condition and span-80 surfactants in organic solvent. Iminodiacetate was first attached to the MNPs through epichlorohydrin agent and then chelated with metal ions. The morphology and chemical properties of these prepared supports were characterized by scanning electron microscopy (SEM), X-ray power diffraction (XRD), vibrating sample magnetometer (VSM), and Fourier transform infrared spectroscopy (FT-IR). Among them, the Co(2+)-chelated AMNPs (AMNPs-ECH-IDA-Co(2+)) showed the second highest enzyme adsorption capacity of 1.81 mg/g particles, and achieved the largest activity recovery of 117% per protein gram in immobilization of ß-glucosidase (BGL). The Michaelis constant (Km) and Vmax of the immobilized BGL were 0.904 mM and 0.057 µmol/min, respectively, and its activation energy was much lower than the free form. Moreover, the immobilized enzyme exhibited enhanced thermostability and operational stability. It still retained more than 90% of its initial activity after being operated for 15 successive batches. This study demonstrates that the immobilized ß-glucosidase has a good prospect in industrial applications.


Assuntos
Enzimas Imobilizadas/metabolismo , Nanopartículas de Magnetita/química , Proteínas de Plantas/metabolismo , beta-Glucosidase/metabolismo , Adsorção , Catálise , Cátions Bivalentes/química , Cobalto/química , Ativação Enzimática , Concentração de Íons de Hidrogênio , Microbiologia Industrial/métodos , Quelantes de Ferro , Cinética , Microscopia Eletrônica de Varredura , Modelos Moleculares , Tamanho da Partícula , Conformação Proteica , Estabilidade Proteica , Prunus/enzimologia , Sefarose/química , Espectroscopia de Infravermelho com Transformada de Fourier , Temperatura , Difração de Raios X
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