Modification of Fe3O4 magnetic nanoparticles by L-dopa or dopamine as an enzyme support

Hong Peng , Xiao Zhang , Kaixun Huang , Huibi Xu

Journal of Wuhan University of Technology Materials Science Edition ›› 2008, Vol. 23 ›› Issue (4) : 480 -485.

PDF
Journal of Wuhan University of Technology Materials Science Edition ›› 2008, Vol. 23 ›› Issue (4) : 480 -485. DOI: 10.1007/s11595-006-4480-5
Article

Modification of Fe3O4 magnetic nanoparticles by L-dopa or dopamine as an enzyme support

Author information +
History +
PDF

Abstract

Fe3O4 magnetic nanoparticles were prepared by co-precipitation of Fe2+ and Fe3+ in an ammonia solution, and its size was about 36 nm measured by an atomic force microscope. Fe3O4 magnetic nanoparticles were modified by L-dopa or dopamine using sonication method. The analysis of FTIR clearly indicated the formation of Fe-O-C bond. Direct immobilization of trypsin (EC: 3.4.21.4) on Fe3O4 magnetic nanoparticles with L-dopa and dopamine spacer was investigated using glutaraldehyde as a coupling agent. No significant changes in the size and magnetic property of the three kinds of magnetic nanoparticles linked with or without trypsin were observed. The existence of the spacer molecule on magnetic nanoparticles could greatly improve the activity and the storage stability of bound trypsin through increasing the flexibility of enzyme and changing the microenvironment on nanoparticles surface compared to the naked magnetic nanoparticles.

Keywords

Fe3O4 magnetic nanoparticles / modification / trypsin / immobilization / L-dopa / dopamine

Cite this article

Download citation ▾
Hong Peng, Xiao Zhang, Kaixun Huang, Huibi Xu. Modification of Fe3O4 magnetic nanoparticles by L-dopa or dopamine as an enzyme support. Journal of Wuhan University of Technology Materials Science Edition, 2008, 23(4): 480-485 DOI:10.1007/s11595-006-4480-5

登录浏览全文

4963

注册一个新账户 忘记密码

References

[1]

Tong X. D., Xue B., Sun Y. A Novel Magnetic Affinity Support for Protein Adsorption and Purification[J]. Biotechnol. Prog., 2001, 17: 134-139.

[2]

Bílková Z., Slováková M., Lyčka A., . Oriented Immobilization of Galactose Oxidase to Bead and Magnetic Bead Cellulose and Poly (HEMA-co-EDMA) and Magnetic Poly (HEMA-co-EDMA) Microspheres[J]. J. Chromatogr. B, 2002, 770: 25-34.

[3]

Jiang D. S., Long S. Y., Huang J., . Immobilization of Pycnoporus Sanguineus Laccase on Magnetic Chitosan Microspheres[J]. Biochem. Eng. J., 2005, 25: 15-23.

[4]

Arica M. Y., Yavuz H., Patir S., . Immobilization of Glucoamylase onto Spacer-arm Attached Magnetic Poly (methylmethacrylate) Microspheres: Characterization and Application to a Continuous Flow Reactor[J]. J. Mol. Catal. B-Enzym., 2000, 11: 127-138.

[5]

Guo Z., Bai S., Sun Y. Preparation and Characterization of Immobilized Lipase on Magnetic Hydrophobic Microspheres[J]. Enzyme Microb. Technol., 2003, 32: 776-782.

[6]

Dyal A., Loos K., Noto M., . Activity of Candida Rugosa Lipase Immobilized on γ-Fe2O3 Magnetic Nanoparticles[J]. J. Am. Chem. Soc., 2003, 125: 1684-1685.

[7]

Xu C. J., Xu K. M., Gu H. W., . Dopamine as A Robust Anchor to Immobilize Functional Molecules on the Iron Oxide Shell of Magnetic Nanoparticles[J]. J. Am. Chem. Soc., 2004, 126: 9938-9939.

[8]

Huang S. H., Liao M. H., Chen D. H. Direct Binding and Characterization of Lipase onto Magnetic Nanoparticles[J]. Biotechnol. Prog., 2003, 19: 1095-1100.

[9]

Koneracká M., Kopčanský P., Timko M., . Direct Binding Procedure of Proteins and Enzymes to Fine Magnetic Particles[J]. J. Mag. Mag. Mat., 2002, 252: 409-411.

[10]

Nouaimi M., Möschel K., Bisswanger H. Immobilization of Trypsin on Polyester Fleece via Different Spacers[J]. Enzyme Microb. Technol., 2001, 29: 567-574.

[11]

Liu X. Q., Zheng H. M., Lai Q. Y., . Synthesis and Characterization of Magnetic Polymer Microspheres with Surface Carboxyl Groups[J]. Chin. J. Inorg. Chem., 2005, 21: 490-494.

AI Summary AI Mindmap
PDF

119

Accesses

0

Citation

Detail

Sections
Recommended

AI思维导图

/