Method for the stabilization and immobilization of enzymatic extracts and its application to the decolorization of textile dyes

Vásquez C.; Anderson D.; Oyarzún M.; Carvajal A.; Palma C.

Abstract

Peroxidases from Pleurotus eryngii have been investigated for their ability to degrade recalcitrant, phenolic pollutants. The use of crude enzymatic extracts can reduce the high costs associated with enzyme purification, and enzyme immobilization can enhance enzyme stability and recovery. The present study tests the effectiveness of various conditions for crude enzyme stabilization in polyethylene glycol and glycine solutions, and immobilization on monofunctional and heterofunctional agarose solid supports. Glycine at 0.5 M at 4 A degrees C and pH 4 was most effective stabilization agent for the crude enzymatic extracts, and enzyme immobilization efficiency was greatest for heterofunctional supports. MANA-glyoxyl heterofunctional supports were demonstrated to have the greatest enhancement of decolorization (1.3-fold) and velocity of substrate consumption (fivefold). Therefore, the application of crude enzymatic extracts to industrial processes, such as dye decolorization, represents a cost-effective alternative to purified enzymes.

Más información

Título según WOS: Method for the stabilization and immobilization of enzymatic extracts and its application to the decolorization of textile dyes
Título según SCOPUS: Method for the stabilization and immobilization of enzymatic extracts and its application to the decolorization of textile dyes
Título de la Revista: BIOTECHNOLOGY LETTERS
Volumen: 36
Número: 10
Editorial: Springer
Fecha de publicación: 2014
Página de inicio: 1999
Página final: 2010
Idioma: English
DOI:

10.1007/s10529-014-1575-5

Notas: ISI, SCOPUS