Abstract
Siliceous ordered mesoporous materials (OMM) are gaining interest as supports for enzyme immobilization due to their uniform pore size, large surface area, tunable pore network and the introduction of organic components to mesoporous structure. We used SBA-15 type silica materials, which exhibit a regular 2D hexagonal packing of cylindrical mesopores of uniform size, for non-covalent immobilization of laccase. Synthesis conditions were adjusted in order to obtain supports with different particle shape, where those with shorter channels had higher loading capacity. Despite the similar isoelectric points of silica and laccase and the close match between the size of laccase and the pore dimensions of these SBA-15 materials, immobilization was achieved with very low leaching. Surface modification of macro-/mesoporous amorphous silica by grafting of amine moieties was proved to significantly increase the isoelectric point of this support and improve the immobilization yield.
Highlights
Siliceous ordered mesoporous materials (OMMs) are gaining interest as supports for enzyme immobilization because of their uniform and tunable pore size and large surface area, which make them excellent hosts for the adsorption of bulky molecules like enzymes [1,2,3,4,5]
The SBA-15 materials were characterized by X-ray diffraction, scanning and transmission electron microscopy to evaluate the morphology and internal structure of the particles, and nitrogen adsorption, to obtain the textural properties of the supports
Two similar ordered mesoporous materials with well-defined morphologies and highly uniform particle sizes synthesized using surfactant templates in acidic solutions were tested as supports for laccase immobilization
Summary
Siliceous ordered mesoporous materials (OMMs) are gaining interest as supports for enzyme immobilization because of their uniform and tunable pore size and large surface area, which make them excellent hosts for the adsorption of bulky molecules like enzymes [1,2,3,4,5]. Laccases (E.C. 1.10.3.2) are a group of multicopper enzymes of industrial interest that catalyze the oxidation of phenolic compounds such as ortho- and para-diphenols to their corresponding quinones with the concomitant reduction of oxygen to water [14,15,16,17,18] Their potential as biocatalysts for use in several biotechnological processes, in nanobiotechnology applications, in food processing and in green chemistry [19,20,21,22,23,24,25,26] is limited by their low operational stability, mostly due to their rapid inactivation by different factors [12]. The laccase immobilization yields on pure silicas and the functionalized amorphous silica, specific activity measurements as well as enzyme leaching tests of immobilized laccase are reported
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