Ramirez HL, Briones AI, Úbeda J, Arevalo M

Idioma: Ingles.
Referencias bibliográficas: 31
Paginas: 101-104
Archivo PDF: 177.84 Kb.

RESUMEN

Se inmovilizó la pectinasa de Aspergillus niger, por absorción en un soporte de quitina recubierta con alginato. Las condiciones óptimas fueron pH 4.5, incubación 2 h y concentración de proteína 85 µg/mL. El rendimiento de la proteína inmovilizada fue del 70 % y la enzima retuvo el 60 % de su actividad inicial. Se evaluaron el pH óptimo, la termoestabilidad y la reusabilidad, entre otras propiedades de la enzima inmovilizada. La termoestabilidad cambió en 9.7 °C, y la enzima inmovilizada fue 10 veces más estable ante el tratamiento térmico a 50 °C que la enzima nativa. El pH óptimo para la actividad catalítica de la pectinasa inmovilizada y la libre fue el mismo. El biocatalizador retuvo el 50 % de su actividad catalítica original después de 9 ciclos de reuso. El bioconjugado mostró estabilidad operacional y mejoramiento de la termoestabilidad. Estas propiedades son adecuadas para la potencial aplicación de la enzima inmovilizada en la industria de jugos.

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