Immobilization of lipase from Candida rugosa onto mesoporous silica supports. [M.Sc. thesis] | Имобилизација липазе из Candida rugosa на мезопорозним силика носачима. Maгистарски рад
2009
Immobilization of lipase from Candida rugosa was investigated onto mesoporous silica particles with different structures. The best effects were obtained on mesoporous silica particles prepared by precipitation and aggregation of primary particles from highly basic sodium silicate solution and the adsorption efficiency on this material was the highest (about 50;). The adsorption efficiency was smaller (about 24;) on core-shell silica particles due to small shell width which was formed by precipitation of silica nanoparticles on previously synthetisized silica particles (cores). However, very small amount of enzyme was bound on mesoporous silica particles synthetisized by hydrolysis and condenzation of tetraethilortosilicate (about 2;). The FTIR spectra showed that the structural conformation of lipase is retained after adsorption onto mesoporous silica support. Although the efficiency of mesoporous biocatalyst was shown to be lower than that of free enzyme, immobilized enzyme showed enhanced thermal stability and can be desorbed by Triton X-100. Investigating the mechanism of immobilization, it was found that van der Waals forces had to play the important role in the binding process of lipase onto mesoporous silica supports when physical adsorption was involved.
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