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Research Article

Nanomaterials as Matrices for Enzyme Immobilization

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Pages 98-109 | Published online: 19 Oct 2010

Figures & data

Table 1. shows the immobilization of enzymes on different nanomaterials and their application.

Figure 1. Preparation procedure for the magnetically separable biocatalysts. (1) Fe(NO3)3·9H2O, methanol; propionic acid; calcination; (2) octyltrimethoxylsilane, toluene, 120 °C for 24 h; (3) 0.2 g of magnetic foam, 20 mL of 50 mg/mL, 6 h at rt; (4) 0.2 g of hydrophobic magnetic foam, 20 mL of 50 mg/mL, 6 h at rt. (Reproduced from [Citation45] with the permission of Copyright Clearance Center's Rightslink service, Elsevier (http://s100.copyright.com/CustomerAdmin/PLF.jsp?lID=2010051_1274898046362).

Figure 1. Preparation procedure for the magnetically separable biocatalysts. (1) Fe(NO3)3·9H2O, methanol; propionic acid; calcination; (2) octyltrimethoxylsilane, toluene, 120 °C for 24 h; (3) 0.2 g of magnetic foam, 20 mL of 50 mg/mL, 6 h at rt; (4) 0.2 g of hydrophobic magnetic foam, 20 mL of 50 mg/mL, 6 h at rt. (Reproduced from [Citation45] with the permission of Copyright Clearance Center's Rightslink service, Elsevier (http://s100.copyright.com/CustomerAdmin/PLF.jsp?lID=2010051_1274898046362).

Figure 2. TEM images of: (a) MWNTs; (b) Candida rugosa lipase CRL absorbed on MWNTs. The diameters of the nanotubes without enzyme were 20 ± 5 nm and with enzyme 30 ± 5 nm (the diameter values represent the average of 10 TEM images in each case). Reproduced from [Citation61] with the permission of BioMed Central (http://creativecommons.org/licenses/by/2.0).

Figure 2. TEM images of: (a) MWNTs; (b) Candida rugosa lipase CRL absorbed on MWNTs. The diameters of the nanotubes without enzyme were 20 ± 5 nm and with enzyme 30 ± 5 nm (the diameter values represent the average of 10 TEM images in each case). Reproduced from [Citation61] with the permission of BioMed Central (http://creativecommons.org/licenses/by/2.0).

Figure 3. TiO2 nanoparticles as synthetic chaperones. Thermally denatured basic proteins interacted with TiO2 nanoparticles. This interaction prevented protein aggregation and facilitated correct refolding of the protein molecules. Reproduced from [Citation71] with the permission of Royal Society of Chemistry, London.

Figure 3. TiO2 nanoparticles as synthetic chaperones. Thermally denatured basic proteins interacted with TiO2 nanoparticles. This interaction prevented protein aggregation and facilitated correct refolding of the protein molecules. Reproduced from [Citation71] with the permission of Royal Society of Chemistry, London.

Figure 4. Affinity layering by bioaffinity immobilization. The lectin concanavalin A (Con A) was bound to its affinity matrix Sephadex G-100. Horseradish Peroxidase (HRP) is a glycoenzyme with known affinity for the lectin and hence was immobilized on Con A-sephadex G-100 by bioaffinity immobilization. In subsequent steps (in which Con A acted as the affinity ligand), alternate layers of Con A and HRP were created. This “going vertical” of affinity layering is a promising strategy for depositing large amount of biological activity on a small surface (for further details about this work, please see reference [Citation82]).

Figure 4. Affinity layering by bioaffinity immobilization. The lectin concanavalin A (Con A) was bound to its affinity matrix Sephadex G-100. Horseradish Peroxidase (HRP) is a glycoenzyme with known affinity for the lectin and hence was immobilized on Con A-sephadex G-100 by bioaffinity immobilization. In subsequent steps (in which Con A acted as the affinity ligand), alternate layers of Con A and HRP were created. This “going vertical” of affinity layering is a promising strategy for depositing large amount of biological activity on a small surface (for further details about this work, please see reference [Citation82]).

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