Puede utilizar el filtro de búsqueda del panel izquierdo para acotar los resultados
Filtro
Tipo de publicación
Todos Libros Revistas
Título
Autor
Palabras clave
ISBN
Acceso DOI
Acceso digital CSIC
Buscar
Datos técnicos
RevistaJournal of Biochemistry
Año2013
Volumen154 (3)
Páginas275-280.
Internacional

Co-immobilization of fungal endo-xylanase and α-L-arabinofuranosidase in glyoxyl agarose for improved hydrolysis of arabinoxylan

Autores:PUBLICACIONES
Grupos de investigación:Ingeniería Enzimática
Plant cell-wall arabinoxylans have a complex structure that requires the action of a pool of debranching (arabinofuranosidases) and depolymerizing enzymes (endo-xylanase). Two Aspergillus nidulans strains over-secreting endo-xylanase and arabinofuranosidase were inoculated in defined 2% maltose-minimum medium resulting in the simultaneously production of these enzymes. To study the synergistic hydrolysis was used arabinoxylan with 41% of arabinose and 59% of xylose residues. Thus, it was adopted different approaches to arabinoxylan hydrolysis using immobilized arabinofuranosidase and endo-xylanase: (i) endo-xylanase immobilized on glyoxyl agarose; (ii) arabinofuranosidase immobilized on glyoxyl agarose; (T1) hydrolysis of arabinoxylan with arabinofuranosidase immobilized on glyoxyl agarose for debranching, followed by a second hydrolysis with endo-xylanase immobilized on glyoxyl agarose; (T2) hydrolysis using (i) and (ii) simultaneously; and (T3) hydrolysis of arabinoxylan with endo-xylanase and arabinofuranosidase co-immobilized on glyoxyl agarose. It was concluded that arabinoxylan hydrolysis using two derivatives simultaneously (T2) showed greater hydrolytic efficiency and consequently a higher products yield. However, the hydrolysis with multi-enzymatic derivative (T3) results in direct release of xylose and arabinose from a complex substrate as arabinoxylan, which is a great advantage as biotechnological application of this derivative, especially regarding the application of biofuels, since these monosaccharides are readily assimilable for fermentation and ethanol production. © The Authors 2013. Published by Oxford University Press on behalf of the Japanese Biochemical Society. 
Palabras clave:
logo de CSIC