Hostname: page-component-76fb5796d-skm99 Total loading time: 0 Render date: 2024-04-26T19:11:18.364Z Has data issue: false hasContentIssue false

Immobilization of hemoglobin on stable mesoporous multilamellar silica vesicles and their activity and stability

Published online by Cambridge University Press:  03 March 2011

Yufang Zhu
Affiliation:
State Key Laboratory of High Performance Ceramics and Superfine Microstructures, Shanghai Institute of Ceramics, Chinese Academy of Sciences, Shanghai 200050, People’s Republic of China
Weihua Shen
Affiliation:
State Key Laboratory of High Performance Ceramics and Superfine Microstructures, Shanghai Institute of Ceramics, Chinese Academy of Sciences, Shanghai 200050, People’s Republic of China
Xiaoping Dong
Affiliation:
State Key Laboratory of High Performance Ceramics and Superfine Microstructures, Shanghai Institute of Ceramics, Chinese Academy of Sciences, Shanghai 200050, People’s Republic of China
Jianlin Shi*
Affiliation:
State Key Laboratory of High Performance Ceramics and Superfine Microstructures, Shanghai Institute of Ceramics, Chinese Academy of Sciences, Shanghai 200050, People’s Republic of China
*
a)Address all correspondence to this author. e-mail: jlshi@sunm.shcnc.ac.cn
Get access

Abstract

A stable mesoporous multilamellar silica vesicle (MSV) was developed with a gallery pore size of about 14.0 nm. A simulative enzyme, hemoglobin (Hb), was immobilized on this newly developed MSV and a conventional mesoporous silica material SBA-15. The structures and the immobilization of Hb on the mesoporous supports were characterized with x-ray diffraction, transmission electron microscopy, N2 adsorption-desorption isotherms, Fourier transform infrared, ultraviolet-visible spectroscopy, and so forth. MSV is a promising support for immobilizing Hb due to its large pore size and high Hb immobilization capacity (up to 522 mg/g) compared to SBA-15 (236 mg/g). Less than 5% Hb was leached from Hb/MSV at pH 6.0. The activity study indicated that the immobilized Hb retained most peroxidase activity compared to free Hb. Thermal stability of the immobilized Hb was improved by the proctetive environment of MSV and SBA-15. Such an Hb-mesoporous support with high Hb immobilization capacity, high activity, and enhanced thermal stability will be attractive for practical applications.

Type
Articles
Copyright
Copyright © Materials Research Society 2005

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1Gorton, L., Marko-Varga, G., Dominguez, E. and Emneus, J. Preface, in Analytical Application of Immobilized Enzyme Reactors, edited by Lam, S. and Malikin, G. (Blackie Academic & Professional, New York, 1994), p. 1.Google Scholar
2Pessiki, P.J., Khangulov, S.V., Ho, D.M. and Dismukes, G.C.: Structural and functional models of the dimanganese catalase enzymes: 2. Structure, electrochemical, redox, and EPR properties. J. Am. Chem. Soc. 116, 891 (1994).CrossRefGoogle Scholar
3Fang, J. and Knobler, C.M.: Phase-separated two-component self-assembled organosilane monolayers and their use in selective adsorption of a protein. Langmuir 12, 1368 (1996).CrossRefGoogle Scholar
4Mrksich, M., Sigal, G.B. and Whitesides, G.M.: Surface plasmon resonance permits in situ measurement of protein adsorption on self-assembled monolayers of alkanethiolates on gold. Langmuir 11, 4383 (1995).CrossRefGoogle Scholar
5Petri, A., Gambicorti, T. and Salvadori, P.: Covalent immobilization of chloroperoxidase on silica gel and properties of the immobilized biocatalyst. J. Mol. Catal. B: Enzym. 27, 103 (2004).CrossRefGoogle Scholar
6Maury, S., Buisson, P. and Pierre, A.C.: Porous texture modification of silica aerogels in liquid media and its effect on the activity of a lipase. Langmuir 17, 6443 (2001).CrossRefGoogle Scholar
7Han, Y., Watson, J.T., Stucky, G.D. and Butler, A.: Catalytic activity of mesoporous silicate-immobilized chloroperoxidase. J. Mol. Catal. B: Enzym. 17, 1 (2002).CrossRefGoogle Scholar
8Deere, J., Magner, E., Wall, J.G. and Hodnett, B.K.: Mechanistic and structural features of protein adsorption onto mesoporous silicates. J. Phys. Chem. B 106, 7340 (2002).CrossRefGoogle Scholar
9Kumar, C.V. and Mclendon, G.L.: Nanoencapsulation of cytochrome c and horseradish peroxidase at the galleries of α-zirconium phosphate. Chem. Mater. 9, 863 (1997).CrossRefGoogle Scholar
10Kumar, C.V. and Chaudhari, A.: Proteins ommobilized at the galleries of layered α-zirconium phosphate: structure and activity studies. J. Am. Chem. Soc. 122, 830 (2000).CrossRefGoogle Scholar
11Diaz, J.F. and Balkus, K.J.: Enzyme immobilization in MCM-41 molecular sieve. J. Mol. Catal. B: Enzym. 2, 115 (1996).CrossRefGoogle Scholar
12Ma, H., He, J., Evans, D.G. and Duan, X.: Immobilization of lipase in a mesoporous reactor based on MCM-41. J. Mol. Catal. B: Enzym. 30, 209 (2004).CrossRefGoogle Scholar
13Gao, L., Bornscheuer, U.T. and Schmid, R.D.: Lipase-catalyzed solid-phase synthesis of sugar esters. Influence of immobilization on productivity and stability of the enzyme. J. Mol. Catal. B: Enzym. 3–4, 279 (1999).Google Scholar
14Reetz, M.T., Zonta, A. and Simpelkamp, J.: Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials. Biotechnol. Bioeng. 49, 527 (1999).3.0.CO;2-L>CrossRefGoogle Scholar
15Nguyen, D., Smit, M., Dunn, B. and Zink, J.L.: Stabilization of creatine kinase encapsulated in silicate sol-gel materials and unusual temperature effects on its activity. Chem. Mater. 14, 4300 (2002).CrossRefGoogle Scholar
16Yiu, H.P., Wright, P.A. and Botting, N.P.: Enzyme immobilization using SBA-15 mesoporous molecular sieves with functionalised surfaces. J. Mol. Catal. B: Enzym. 15, 81 (2001).CrossRefGoogle Scholar
17Yiu, H.P., Botting, C.H., Botting, N.P.J. and Wright, P.A.: Size selective protein adsorption on thiol-functionalised SBA-15 mesoporous molecular sieve. Phys. Chem. Chem. Phys. 3, 2983 (2001).CrossRefGoogle Scholar
18Yiu, H.P., Wright, P.A. and Botting, N.P.J.: Enzyme immobilisation using siliceous mesoporous molecular sieves. Micro. Meso. Mater. 44-45, 763 (2001).CrossRefGoogle Scholar
19Takahashi, H., Li, B., Sasaki, T., Miyazaki, C., Kajino, T. and Inagaki, S.: Catalytic activity in organic solvents and stability of immobilized enzymes depend on the pore size and surface characteristics of mesoporous silica. Chem. Mater. 12, 3301 (2000).CrossRefGoogle Scholar
20Takahashi, H., Li, B., Sasaki, T., Miyazaki, C., Kajino, T. and Inagaki, S.: Immobilized enzymes in orderd mesoporous silica materials and improvement of their stability and catalytic activity in an organic solvent. Micro. Meso. Mater. 44-45, 755 (2001).CrossRefGoogle Scholar
21He, J., Li, X., Evans, D.G., Duan, X. and Li, C.: A new support for the immobilization of penicillin acylase. J. Mol. Catal., B: Enzym. 11, 45 (2000).CrossRefGoogle Scholar
22Pandya, P.H., Jasra, R.V., Newalker, B.L. and Bhatt, P.N.: Studies on the activity and stability of immobilized α-amylase in ordered mesoporous silicas. Micro. Meso. Mater. 77, 67 (2004).CrossRefGoogle Scholar
23Fan, J., Lei, J., Wang, L., Yu, C., Tu, B. and Zhao, D.: Rapid and high capacity immobilization of enzymes based on mesoporous silicas with controlled morphologies. Chem. Comm. 2140 (2003).CrossRefGoogle ScholarPubMed
24Kumar, C.V. and Chaudhari, A.: Efficient renaturation of immobilized met-hemoglobin at the galleries of α-zirconium phosphonate. Chem. Mater. 13, 238 (2001).CrossRefGoogle Scholar
25Geng, L., Li, N., Dai, N., Wen, X., Zhao, F. and Li, K.: Layered γ-zirconium phosphate a new matrix for immobilization of hemoglobin. Colloids Surf. B 29, 81 (2003).CrossRefGoogle Scholar
26Zhao, D., Huo, Q., Feng, J., Chmelka, B.F. and Stucky, G.D.: Nonionic triblock and star diblock copolymer and oligomeric surfactant syntheses of highly ordered, hydrothermally stable, mesoporous silica structures. J. Am. Chem. Soc. 120, 6024 (1998).CrossRefGoogle Scholar
27Marshall, A.G.: Biophysical Chemistry, Principles, Techniques, and Applications, (Wiley & Sons, New York, 1978), p. 70.Google Scholar
28Kim, S.S., Zhang, W.Z. and Pannavaia, T.J.: Ultrastable mesostructured silica vesicles. Science 282, 1302 (1998).CrossRefGoogle ScholarPubMed
29Tanev, P.T. and Pannavaia, T.J.: Biomimetic templating of porous lamellar silicas by vesicular surfactant assemblies. Science 271, 1267 (1996).CrossRefGoogle Scholar
30Tanev, P.T., Liang, Y. and Pannavaia, T.J.: Assembly of mesoporous lamellar silicas with hierarchical particle architectures. J. Am. Chem. Soc. 119, 8616 (1997).CrossRefGoogle Scholar
31Wang, J., Larsen, R.W., Moench, S.J., Satterlee, J.D., Rousseau, D.L. and Ondrias, M.R.: Cytochrome c peroxidase complexed with cytochrome c has an unperturbed heme moiety. Biochemistry 35, 453 (1996).CrossRefGoogle ScholarPubMed
32Smith, H.T. and Millett, F.: Involvement of lysines-72 and -79 in the alkaline isomerization of horse heart ferricytochrome c. Biochemistry 19, 1117 (1980).CrossRefGoogle ScholarPubMed
33Torii, H. and Tasumi, M.: Infrared Spectroscopy of Biomoleculaes, edited by Mantsh, H.H. and Chapman, D. (John Wiley & Sons, New York, 1996), pp. 118.Google Scholar
34Peng, S., Gao, Q., Wang, Q. and Shi, J.: Layered structural heme protein magadiite nanocomposites with high enzyme-like peroxidase activity. Chem. Mater. 16, 2675 (2004).CrossRefGoogle Scholar
35Kosmulski, M.J.: pH-dependent surface charging and points of zero charge II. Update. J. Colloid Interface Sci. 275, 214 (2004).CrossRefGoogle ScholarPubMed
36Dong, A., Huang, P. and Caughey, W.S.: Redox-dependent changes in beta.-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra. Biochemistry 31, 182 (1992).CrossRefGoogle ScholarPubMed
37Wang, X.: Biochemistry, 1st ed. (Tsinghua University Publishing Company, Beijing, China, 2001), p. 69.Google Scholar