Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.apsusc.2004.06.080
Title: Functionalized nanoporous silicas for the immobilization of penicillin acylase
Authors: Maria Chong, A.S.
Zhao, X.S. 
Keywords: Co-condensation
Enzyme immobilization
Enzyme-support interactions
Mesoporous silica
SBA-15
Surface functionalization
Issue Date: 15-Oct-2004
Source: Maria Chong, A.S., Zhao, X.S. (2004-10-15). Functionalized nanoporous silicas for the immobilization of penicillin acylase. Applied Surface Science 237 (1-4) : 398-404. ScholarBank@NUS Repository. https://doi.org/10.1016/j.apsusc.2004.06.080
Abstract: Nanoporous silica materials with uniform pore size and ordered structure have drawn growing interest of researchers since 1990s. A large-pore nanoporous material, SBA-15, was functionalized with organosilanes by co-condensation method in the presence of nonionic triblock copolymer P123 as a template under acidic conditions. The functionalization was demonstrated by using five organosilanes, namely 3-aminopropyltriethoxysilane (APTES), 3- mercaptopropyltrimethoxysilane (MPTMS), phenyltrimethoxysilane (PTMS), vinyltriethoxysilane (VTES), and 4-(triethoxysilyl)butyronitrile (TSBN), which modified the surface properties of the silica materials, enabling the materials to be a promising support for immobilization of biological molecules. The functionalized SBA-15 materials exhibited long-range ordering of two-dimensional hexagonal pore arrays of size ranging from 66 to 90Å as demonstrated by small-angle X-ray scattering (SAXS), transmission electron microscopy (TEM), and physical adsorption techniques. A variety of organosilane density in the range of 0.5-2.6mmol/g was achieved as revealed by elemental analysis and solid-state nuclear magnetic resonance (NMR) techniques. The functionalized materials displayed improved properties for immobilization of penicillin acylase (PA) in comparison with pure-silica SBA-15. Such improvement is believed to be due to the enhanced surface hydrophobicity and electrostatic interactions of the functional groups with the enzyme. © 2004 Elsevier B.V. All rights reserved.
Source Title: Applied Surface Science
URI: http://scholarbank.nus.edu.sg/handle/10635/74602
ISSN: 01694332
DOI: 10.1016/j.apsusc.2004.06.080
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