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Optical Sol-Gel Materials Based on Binding and Catalysis by Biomolecules

Published online by Cambridge University Press:  21 February 2011

Jeffrey I. Zink ,
Bruce Dunn ,
Stacey Yamanaka ,
Esther Lan ,
J. S. Valentine  and
K. E. Chung
Jeffrey I. Zink
Affiliation:
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024
Bruce Dunn
Affiliation:
Department of Materials Science and Engineering, University of California, Los Angeles, CA 90024
Stacey Yamanaka
Affiliation:
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024
Esther Lan
Affiliation:
Department of Materials Science and Engineering, University of California, Los Angeles, CA 90024
J. S. Valentine
Affiliation:
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024
K. E. Chung
Affiliation:
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024
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Abstract

The proteins copper-zinc Superoxide dismutase (CuZnSOD), cytochrome c, myoglobin, hemoglobin, and bacterio-rhodopsin are encapsulated in stable, optically transparent, porous, silica glass matrices prepared by the sol-gel method such that the biomolecules retain their characteristic reactivities and spectroscopic properties. The resulting glasses allow transport of small molecules into and out of the glasses at reasonable rates but retain the protein molecules within their pores. The transparency of the glasses enables the chemical reactions of the immobilized proteins to be monitored by means of changes in their visible absorption spectra. Silica glasses containing the immobilized proteins have similar reactivities and spectroscopic properties to those found for the proteins in solution. The enzymes glucose oxidase and peroxidase were also encapsulated in transparent silica glass matrices. Upon exposure to glucose solutions, a colored glass is formed that can be used as the active element in a solid state optically based glucose sensor. Likewise, gels containing oxalate oxidase and peroxidase exhibit spectroscopic changes upon exposure to aqueous solutions containing oxalic acid.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 346: Symposium N – Better Ceramics Through Chemistry VI , 1994 , 1017
Copyright
Copyright © Materials Research Society 1998

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References

REFERENCES

1 Avnir, D., Brown, S. and Ottolenghi, M., in Supramolecular Architecture in Two and Three Dimensions, edited by Bein, T. (American Chemical Society, New York, 1992).Google Scholar
2 Dunn, B. and Zink, J.I., J. Mater. Chem. 1, 903 (1991).Google Scholar
3 Brinker, C.J., Scherer, G., Sol-Gel Science: The Physics and Chemistry of Sol-Gel Processing (Academic Press, San Diego, 1989).Google Scholar
4 Klein, L.C., Ann. Rev. Mater. Sei. 15, 227 (1985).Google Scholar
5 Pouxviel, J.C., Dunn, B., and Zink, J.I., J. Phys. Chem. 93, 2134 (1989).Google Scholar
6 Slama-Schwok, A., Avnir, D., and Ottolenghi, M., J. Phys. Chem. 93, 7544 (1989).Google Scholar
7 Reisfeld, R., J. Non-Cryst. Solids 121, 254 (1990).Google Scholar
8 Mosbach, K., editor, Immobilized Enzymes and Cells, Part B, Methods in Enzymology (Academic Press, Inc., 1986).Google Scholar
9 Braun, S., Rappopoit, S., Zusman, R., Avnir, D., Ottolenghi, M., Materials Lett. 10, 1 (1990).Google Scholar
10 Ellerby, L.M., Nishida, C.R., Nishida, R., Yamanaka, S.A., Dunn, B., Valentine, J.S., and Zink, J.I., Science 255, 1113 (1992).Google Scholar
11 Yamanaka, S.A., Nishida, F., Ellerby, L.M., Nishida, C.R., Dunn, B., Valentine, J.S., and Zink, J.I., Chem. Mat. 4, 495 (1992).Google Scholar
12 Esquivias, L. and Zarzycki, J., in Proceedings of the Third International Conference on Ultrastructure Processing, edited by Mackenzie, J. D. and Ulrich, D. R. (John Wiley & Sons Inc., New York, 1988), p. 255.Google Scholar
13 Valentine, J. S. and Pantoliano, M. W., in Copper Proteins, edited by Spiro, T. G. (Wiley, New York, 1981) and references therein.Google Scholar
14 Antonini, E., and Brunori, M., Hemoglobin and Myoglobin in Their Reactions with Ligands (North-Holland Publishing Co., Amsterdam, 1971).Google Scholar
15 Birge, R.R., Biochim. Biophys. Acta. 293, 1016 (1990).Google Scholar
16 Birge, R.R., Annu. Rev. Phys. Chem. 41, 683 (1990) and references cited therein.Google Scholar
17 Oesterhelt, D., Brauchle, C., Hampp, N., Quarterly Rev. Biophys. 24, 425 (1991) and references cited therein.Google Scholar
18 Brauchle, C., Hampp, N., Oesterhelt, D., Advanced Materials 3, 420 (1991) and references cited therein.Google Scholar
19 Miyasaka, T., Koyama, K., Itoh, I., Science 255, 342 (1992).Google Scholar
20 van den Berg, R., Jang, D.-J., Bitting, H.C., and El-Sayed, M.A., Biophys. J. 58, 135 (1990).Google Scholar
21 Braun, S., Shtelzer, S., Rappoport, S., Avnir, D., Ottolenghi, M., J. Non-Cryst. Solids 147, 739 (1992).Google Scholar
22 Trinder, P., Ann. Clin. Biochem. 6, 24 (1969).Google Scholar
23 Ngo, T.T., Lenhoff, H.M., Anal. Biochem. 105, 389 (1980).Google Scholar
24 Chiriboga, J., Biochem. and Biophys. Res. Comm. 11, 277 (1963).Google Scholar
25 Suguira, M., Yamamura, H., Hirano, K., Sasaki, M., Morikawa, M., Tsuboi, M., Chem. Pharm. Bull. 27, 2003 (1979).Google Scholar