Artículos de revistas
Simultaneous purification and immobilization of soybean hull peroxidase with a dye attached to chitosan mini-spheres
Fecha
2017-06Registro en:
Bracco, Lautaro Fidel; Levin, Gustavo Javier; Navarro, Agustin Andres; Wolman, Federico Javier; Miranda, Maria Victoria; et al.; Simultaneous purification and immobilization of soybean hull peroxidase with a dye attached to chitosan mini-spheres; Taylor & Francis Ltd; Biocatalysis and Biotransformation; 35; 5; 6-2017; 1-9
1024-2422
CONICET Digital
CONICET
Autor
Bracco, Lautaro Fidel
Levin, Gustavo Javier
Navarro, Agustin Andres
Wolman, Federico Javier
Miranda, Maria Victoria
Cascone, Osvaldo
Resumen
Soybean hull peroxidase (EC 1.11.1.7, SBP) was simultaneously purified and immobilized by dye affinity chromatography with Reactive Blue 4 attached to chitosan mini-spheres. Under optimized conditions, 96% of SBP was adsorbed to the matrix. Under the most stringent condition, only 49% was desorbed, whereas 2 M NaCl failed to desorb a significant amount of SBP. This behaviour allowed proposing the dye matrix as a support to immobilize SBP from a crude extract. The pH of maximum activity shifted from 7 to 3?5. SBP gained thermostability after immobilization: after 5 h at 85 °C, the remaining activity was 54%, whereas that of the free enzyme was 31%. The optimum temperature for the immobilized SBP was 75 °C, whereas that of the free enzyme was 55 °C. After two months at 4 °C, the activity loss of the immobilized SBP was only 3%. Immobilized SBP removed 80% of 2-bromophenol from wastewater in 180 min and, after five cycles of use, the activity loss was only 12.8%.