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Effect of substrate (ZnO) morphology on enzyme immobilization and its catalytic activity.

Zhang Y, Wu H, Huang X, Zhang J, Guo S - Nanoscale Res Lett (2011)

Bottom Line: The control on the morphology of ZnO nanocrystals was achieved by varying the ratio of CH3OH to H2O, which were used as solvents in the hydrothermal reaction system.The surface of as-prepared ZnO nanoparticles was functionalized with amino groups using 3-aminopropyltriethoxysilane and tetraethyl orthosilicate, and the amino groups on the surface were identified and calculated by FT-IR and the Kaiser assay.Horseradish peroxidase was immobilized on as-modified ZnO nanostructures with glutaraldehyde as a crosslinker.

View Article: PubMed Central - HTML - PubMed

Affiliation: National Key Laboratory of Micro/Nano Fabrication Technology, Key Laboratory for Thin Film and Microfabrication of the Ministry of Education, Research Institute of Micro/Nano Science and Technology, Shanghai Jiao Tong University, Shanghai 200240, PR China. haixiawu@sjtu.edu.cn.

ABSTRACT
In this study, zinc oxide (ZnO) nanocrystals with different morphologies were synthesized and used as substrates for enzyme immobilization. The effects of morphology of ZnO nanocrystals on enzyme immobilization and their catalytic activities were investigated. The ZnO nanocrystals were prepared through a hydrothermal procedure using tetramethylammonium hydroxide as a mineralizing agent. The control on the morphology of ZnO nanocrystals was achieved by varying the ratio of CH3OH to H2O, which were used as solvents in the hydrothermal reaction system. The surface of as-prepared ZnO nanoparticles was functionalized with amino groups using 3-aminopropyltriethoxysilane and tetraethyl orthosilicate, and the amino groups on the surface were identified and calculated by FT-IR and the Kaiser assay. Horseradish peroxidase was immobilized on as-modified ZnO nanostructures with glutaraldehyde as a crosslinker. The results showed that three-dimensional nanomultipod is more appropriate for the immobilization of enzyme used further in catalytic reaction.

No MeSH data available.


The enzyme loadings on different morphologies of ZnO nanocrystals. The loadings of HRP with different ratios of glutaraldehyde and amine groups on the surface of the modified ZnO nanocrystals.
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Figure 6: The enzyme loadings on different morphologies of ZnO nanocrystals. The loadings of HRP with different ratios of glutaraldehyde and amine groups on the surface of the modified ZnO nanocrystals.

Mentions: The two aldehyde groups (-COH) of glutaraldehyde can bond separately to the amino groups of HRP and as-modified ZnO [28], and thus, glutaraldehyde was used as a crosslinker to immobilize HRP molecules on the modified ZnO nanocrystal surfaces. As shown in Figure 6, the highest loadings of HRP on the ZnO nanospheres, nanodisks and nanomultipods were 0.094, 0.275, 0.240 mg/m2, respectively From Figure 6, we find that the immobilization of HRP on ZnO nanomultipods can reach the highest loading at the lowest ratio of glutaraldehyde to amino groups. The maximum loading of HRP on ZnO nanomultipods was higher than that on the nanospheres, but, as high as that on the nanodisks, even if the surface density of amino groups on ZnO nanomultipods was relatively lower than that of the other two.


Effect of substrate (ZnO) morphology on enzyme immobilization and its catalytic activity.

Zhang Y, Wu H, Huang X, Zhang J, Guo S - Nanoscale Res Lett (2011)

The enzyme loadings on different morphologies of ZnO nanocrystals. The loadings of HRP with different ratios of glutaraldehyde and amine groups on the surface of the modified ZnO nanocrystals.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3211870&req=5

Figure 6: The enzyme loadings on different morphologies of ZnO nanocrystals. The loadings of HRP with different ratios of glutaraldehyde and amine groups on the surface of the modified ZnO nanocrystals.
Mentions: The two aldehyde groups (-COH) of glutaraldehyde can bond separately to the amino groups of HRP and as-modified ZnO [28], and thus, glutaraldehyde was used as a crosslinker to immobilize HRP molecules on the modified ZnO nanocrystal surfaces. As shown in Figure 6, the highest loadings of HRP on the ZnO nanospheres, nanodisks and nanomultipods were 0.094, 0.275, 0.240 mg/m2, respectively From Figure 6, we find that the immobilization of HRP on ZnO nanomultipods can reach the highest loading at the lowest ratio of glutaraldehyde to amino groups. The maximum loading of HRP on ZnO nanomultipods was higher than that on the nanospheres, but, as high as that on the nanodisks, even if the surface density of amino groups on ZnO nanomultipods was relatively lower than that of the other two.

Bottom Line: The control on the morphology of ZnO nanocrystals was achieved by varying the ratio of CH3OH to H2O, which were used as solvents in the hydrothermal reaction system.The surface of as-prepared ZnO nanoparticles was functionalized with amino groups using 3-aminopropyltriethoxysilane and tetraethyl orthosilicate, and the amino groups on the surface were identified and calculated by FT-IR and the Kaiser assay.Horseradish peroxidase was immobilized on as-modified ZnO nanostructures with glutaraldehyde as a crosslinker.

View Article: PubMed Central - HTML - PubMed

Affiliation: National Key Laboratory of Micro/Nano Fabrication Technology, Key Laboratory for Thin Film and Microfabrication of the Ministry of Education, Research Institute of Micro/Nano Science and Technology, Shanghai Jiao Tong University, Shanghai 200240, PR China. haixiawu@sjtu.edu.cn.

ABSTRACT
In this study, zinc oxide (ZnO) nanocrystals with different morphologies were synthesized and used as substrates for enzyme immobilization. The effects of morphology of ZnO nanocrystals on enzyme immobilization and their catalytic activities were investigated. The ZnO nanocrystals were prepared through a hydrothermal procedure using tetramethylammonium hydroxide as a mineralizing agent. The control on the morphology of ZnO nanocrystals was achieved by varying the ratio of CH3OH to H2O, which were used as solvents in the hydrothermal reaction system. The surface of as-prepared ZnO nanoparticles was functionalized with amino groups using 3-aminopropyltriethoxysilane and tetraethyl orthosilicate, and the amino groups on the surface were identified and calculated by FT-IR and the Kaiser assay. Horseradish peroxidase was immobilized on as-modified ZnO nanostructures with glutaraldehyde as a crosslinker. The results showed that three-dimensional nanomultipod is more appropriate for the immobilization of enzyme used further in catalytic reaction.

No MeSH data available.