Artículos de revistas
Easily handling penicillin G acylase magnetic cross-linked enzymes aggregates: Catalytic and morphological studies
Fecha
2014-01-01Registro en:
Process Biochemistry. Oxford: Elsevier Sci Ltd, v. 49, n. 1, p. 38-46, 2014.
1359-5113
10.1016/j.procbio.2013.09.024
WOS:000331156100006
2115942621694174
0000-0003-0195-3885
Autor
Universidade Federal de São Carlos (UFSCar)
Universidade Estadual Paulista (Unesp)
Institución
Resumen
Biomolecules labeled with superparamagnetic nanoparticles can be selectively removed from complex reaction mixtures using an external magnetic field. Amino-functionalized superparamagnetic iron oxide nanoparticles (amino-SPION) were co-aggregated with penicillin G acylase and then cross-linked, generating magnetic cross-linked enzymes aggregates (M-CLEAs) that were quickly and efficiently recovered from the reaction medium by applying an external magnetic field. M-CLEAs and cross-linked enzymes aggregates (CLEAs) prepared under the same reaction conditions were characterized and compared. The best recovered activities were obtained for M-CLEAs prepared using polyethylene glycol 600 as precipitant and the most stable M-CLEA were obtained using tert-butanol. Successive penicillin G hydrolysis reactions were carried out using the same M-CLEA in a 50 mL reactor (3 reaction cycles), after the reactions the derivate was magnetically recovered without loss of activity demonstrating a total magnetic recovery. Line-scan energy dispersive X-ray spectroscopy showed that the amino-SPIONs were homogeneously dispersed within the structure of the M-CLEA. (C) 2013 Elsevier Ltd. All rights reserved.