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Proceedings Paper

Immobilization of lipase and keratinase on functionalized SBA-15 nanostructured materials
Author(s): Hy G. Le; Tuan A. Vu; Hoa T. K. Tran; Phuong T. Dang
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Paper Abstract

SBA-15 nanostructured materials were synthesized via hydrothermal treatment and were functionalized with 3- aminopropyltriethoxysilane (APTES). The obtained samples were characterized by different techniques such as XRD, BET, TEM, IR and DTA. After functionalization, it showed that these nanostrucrured materials still maintained the hexagonal pore structure of the parent SBA-15. The model enzyms chosen in this study were lipase and keratinase. Lipase was a biocatalyst for hydrolyzation of long chain triglycerides or methyl esters of long chain alcohols and fatty acids; keratinase is a proteolytic enzyme that catalyzes the cleavage of keratin. The functionalized SBA-15 materials were used to immobilize lipase and keratinase, exhibiting higher activity than that of the unfunctionalized pure silica SBA-15 ones. This might be due to the enhancing of surface hydrophobicity upon functionalization. The surface functionalization of the nanostructured silicas with organic groups can favor the interaction between enzyme and the supports and consequently increasing the operational stability of the immobilized enzymes. The loading of lipase on functionalized SBA-15 materials was higher than that of keratinase. This might be rationalized by the difference in size of enzyms.

Paper Details

Date Published: 7 December 2013
PDF: 9 pages
Proc. SPIE 8923, Micro/Nano Materials, Devices, and Systems, 892343 (7 December 2013); doi: 10.1117/12.2033345
Show Author Affiliations
Hy G. Le, Vietnam Academy of Science and Technology (Viet Nam)
Tuan A. Vu, Vietnam Academy of Science and Technology (Viet Nam)
Hoa T. K. Tran, Vietnam Academy of Science and Technology (Viet Nam)
Phuong T. Dang, Vietnam Academy of Science and Technology (Viet Nam)

Published in SPIE Proceedings Vol. 8923:
Micro/Nano Materials, Devices, and Systems
James Friend; H. Hoe Tan, Editor(s)

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