Hierarchical meso-macroporous silica grafted with glyoxyl groups: opportunities for covalent immobilization of enzymes

Bernal, C; Urrutia, P; Illanes A.; Wilson, L

Abstract

Hierarchical meso-macroporous silica (average mesopore diameter 20 nm) was synthesized and chemically modified to be used as a support for the immobilization of lipases from Candida antarctica B and Alcaligenes sp. and beta-galactosidases from Bacillus circulans and Aspergillus oryzae. Catalytic activities and thermal stabilities of enzymes immobilized by multipoint covalent attachment in silica derivatized with glyoxyl groups were compared with those immobilized in glyoxyl-agarose, assessing biocatalyst performance under non-reactive conditions in aqueous medium. In the case of A. oryzae beta-galactosidase and Alcaligenes sp. lipase, an additional step of amination was needed to improve immobilization yield. Specific activities of lipases immobilized in glyoxyl-silica were high (232 and 62 IU per gram, for C. antarctica B and Alcaligenes sp. respectively); thermal stabilities were higher than those immobilized in glyoxyl-agarose. Although in the case of beta-galactosidases from B. circulans and A. oryzae, the specific activities (250 and 310 IU per gram, respectively) were lower than the ones obtained with glyoxyl-agarose, expressed activities were similar to values previously reported. Thermal stabilities of both beta-galactosidases immobilized in glyoxyl-silica were higher than when glyoxyl-agarose was used as support. Results indicate that hierarchical meso-macroporous silica is a versatile support for the production of robust biocatalysts.

Más información

Título según WOS: Hierarchical meso-macroporous silica grafted with glyoxyl groups: opportunities for covalent immobilization of enzymes
Título según SCOPUS: Hierarchical meso-macroporous silica grafted with glyoxyl groups: Opportunities for covalent immobilization of enzymes
Título de la Revista: NEW BIOTECHNOLOGY
Volumen: 30
Número: 5
Editorial: ELSEVIER SCIENCE BV
Fecha de publicación: 2013
Página de inicio: 500
Página final: 506
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S1871678413000149
DOI:

10.1016/j.nbt.2013.01.011

Notas: ISI, SCOPUS