In this article, the authors study the possibility of enzyme immobilization on the nonfunctionalized pure silica SBA-15 as well as functionalized SBA-15 materials. The model enzyme chosen in this study was D-amino acid oxidase (DAAO) and lipase (EC 3.1.1.3). DAAO was industrially important enzyme for the production of glutaryl 7-amino cephalosporanic acid (GL-7-ACA) from cephalosporin C (CPC); Lipase is the catalyst hydrolysis long chain triglycerides or methyl esters of long chain alcohols and fatty acids. Substances formed are 1-2 or 2-3 diglyxerit; 2-monoglyxerit; 1 or 3-mono glyceride and glixerol. The obtained results showed that functionalized SBA-15 materials exhibited higher enzymatic activity and stability than that of non-functionalized one. However, the loading of enzyme of these materials for lipase is about 1.5 times greater than DAAO. This might be due to the fact that the size of the lipase (3.5 x 3.6 x 4.2 nm) is smaller than the size of DAAO (11.2 x 4.5 x 3.1 nm) and smaller than the capillary size of the non-functional (8.7 nm) and functional (6.9 nm), so they are easily diffused and fixed onto the inside of the capillary carrier.
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