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Abstract
Mesoporous silica particles for immobilization of lipase from Candida rugosa were prepared by precipitation and aggregation of primary particles from highly basic sodium silicate solution but without addition of templates. The average pore size of the material was 15.8 nm, which allowed enzyme adsorption inside the pores and high enzyme loading. Specific surface area of the material was found to be 359 m2g−1. A loading of 100 mglipasegdrysilica−1 was obtained at initial enzyme concentration of 1.8 mgmL−1 by physical adsorption. The FTIR spectrum showed the structural conformation of lipase to be retained after adsorption into the mesoporous silica support. Although the efficiency of the mesoporous biocatalyst was shown to be lower than that of the free enzyme, the immobilized enzyme showed enhanced thermal stability and could be desorbed with Triton X-100, indicating the hydrophobic nature of the adsorption.
Acknowledgements
This work was supported by the Serbian Ministry of Science and Technological Development, Project ‘Synthesis of nanopowders and processing of ceramics and nanocomposites for application in novel technologies’, No. 142059.