Abstract
Mesoporous silica materials are attractive materials for immobilizing enzymes because of their well-ordered structures, large surface area are pore volume. Diffusion of large enzyme molecules such as porcine pancreatic lipase (PPL) through the lengthy channels of MPS takes place too slowly. Therefore, the squat of the enzyme at the pore mouth entrance, actually makes the rest of the channel useless. In this study, to overcome this problem, synthesis parameters of SBA-15 were changed, since along with pore diameter increasing, the mesochannel length becomes shorter. The main point to obtain a well-ordered 2D hexagonal pore structure was the pre-hydrolysis of tetraethyl orthosilicate (TEOS) before the addition of 1,3,5-trimethyl benzene as a micelle swelling agent. Due to the strong effect of zirconium in changing the morphology of SBA-15 particles, we modified SBA-15 in the presence of a small amount of ZrOCl2 in the synthesis solution under acidic conditions. As a result, mesochannel length of SBA-15-Zr was shortened from 600 to <200 nm. The morphology of mesoporous silica was also changed from rod-like to platelet, because of the accelerating effect of Zr(IV) on the self-assembly rate of P123 and TEOS condensation. Characteristic results conducted by low angle XRD, high resolution transmission electron microscopy and nitrogen adsorption, confirmed tuning effect of Zr(IV) in SBA-15. Furthermore, it was shown that the number of pore entrances increases with decreasing the length of SBA-15 mesochannels, leading to obvious improvement of enzyme uptake. PPL has been successfully immobilized in the mesoporous channels of SBA-15-Zr. The total amount of lipase adsorbed on the mesoporous SBA-15-Zr was measured by thermal gravimetric analysis. The largest PPL adsorption capacity was 784 mg/g belonging to the SBA-15-Zr with the length of 150 nm and the mean pore size diameter of 9.22 nm.
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