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

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 β-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 β-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 β-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 β-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.

► Lipases and β-galactosidases were efficiently immobilized in glyoxyl porous silica.
► Silica was compared with agarose in terms of catalytic activity and thermal stability.
► Activities of lipase immobilized in silica were higher than in agarose based supports.
► Independent of the kind of enzyme, thermal stability was notably higher in silica.
► Meso-macroporous silica is a versatile support for robust biocatalysts production.