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Encapsulation and Reactivity of Proteins in Optically Transparent Porous Silicate Glasses Prepared by the Sol-Gel Method

Published online by Cambridge University Press:  15 February 2011

Stacey A. Yamanaka ,
Lisa M. Ellerby ,
Ester H. Lan ,
Clinton R. Nishida ,
Fumito Nishida ,
Bruce Dunn ,
Joan Selverstone Valentine  and
Jeffrey I. Zink
Stacey A. Yamanaka
Affiliation:
University of California, Los Angeles, Dept. of Chemistry and Biochemistry, Los Angeles, CA 90024
Lisa M. Ellerby
Affiliation:
University of California, Los Angeles, Dept. of Chemistry and Biochemistry, Los Angeles, CA 90024
Ester H. Lan
Affiliation:
University of California, Los Angeles, Dept. of Materials Science and Engineering, Los Angeles, CA 90024
Clinton R. Nishida
Affiliation:
University of California, Los Angeles, Dept. of Chemistry and Biochemistry, Los Angeles, CA 90024
Fumito Nishida
Affiliation:
University of California, Los Angeles, Dept. of Materials Science and Engineering, Los Angeles, CA 90024
Bruce Dunn
Affiliation:
University of California, Los Angeles, Dept. of Materials Science and Engineering, Los Angeles, CA 90024
Joan Selverstone Valentine
Affiliation:
University of California, Los Angeles, Dept. of Chemistry and Biochemistry, Los Angeles, CA 90024
Jeffrey I. Zink
Affiliation:
University of California, Los Angeles, Dept. of Chemistry and Biochemistry, Los Angeles, CA 90024
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Abstract

Copper-zinc superoxide dismutase (CuZnSOD), myoglobin, hemoglobin and glucose oxidase are encapsulated in stable, optically transparent, porous, silica glass matrices synthesized under mild conditions using novel sol-gel synthetic techniques. The biomolecules retain their characteristic reactivities and spectroscopic properties. The porous glasses allow transport of small molecules into and out of the glasses at reasonable rates but retain the protein molecules within the pores. The chemical reactions of the immobilized proteins are monitored by means of changes in their visible absorption spectra. Four encapsulated proteins are studied: CuZnSOD reacts with CN−; metmyoglobin is reduced to its deoxy form and then reacts with O2 to make the oxy form and CO to make the carbonyl form; methemoglobin is reduced to its deoxy form and reacted with CO to make the carbonyl form; and glucose oxidase is reacted with glucose to make gluconic acid.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 277: Symposium V – Macromolecular Host-Guest Complexes: Optical, Optoelectronic, and Photorefractive Properties and Applications , 1992 , 99
Copyright
Copyright © Materials Research Society 1992

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References

REFERENCES

1) Brinker, C.J. and Scherer, G., Sol-Gel Science: The Physics and Chemistry of Sol-Gel Processing (Academic Press, Boston, 1990).Google Scholar
2) McKiernan, a. J.M., Pouxviel, J.C., Dunn, B., and Zink, J.I., J. Phys. Chem. 93, 2129 (1989). b. J.C. Pouxviel, B. Dunn, and J.I. Zink, J. Phys. Chem. 93, 2134, (1989). c. J.M. McKiernan, S.A. Yamanaka, B. Dunn, and J.I. Zink, J. Phys. Chem. 94, 5652 (1990). d. E.T. Knobbe, P.D. Fuqua, F. Nishida, and B. Dunn, Appl. Opt. 22, 2729 (1990). e. B. Dunn and J.I. Zink, J. Mater. Chem., 903 (1991). f. J. M. McKiernan, S.A. Yamanaka, E. Knobbe, J.C. Pouxviel, S. Parveneh, B. Dunn, and J.I. Zink, J. Inorg. Organomet. Polym. 1, 87 (1991).Google Scholar
3) Braun, S., Rappoport, S., Zusman, R., Avnir, D., and Ottolenghi, M., Mater. Lett. 10, 1 (1990).Google Scholar
4) Esquivias, L. and Zarzycki, J. in Proceedings of the Third International Conference on Ultrastructure Processing, edited by Mackenzie, J.D. and Ulrich, D.R. (Wiley, New York, 1988) pp. 255–270.Google Scholar
5) Ellerby, a. L.M., Nishida, C.R., Nishida, F., Yamanaka, S.A., Dunn, B., Valentine, J.S., and Zink, J.I. Science, 75L 1113 (1992). b. S.A. Yamanaka, F. Nishida, L.M. Ellerby, C.R. Nishida, B. Dunn, J.S. Valentine, and J.I. Zink, Chem. Mat., in press.Google Scholar
6) Valentine, J.S. and Pantoliano, M.W., Copper Proteins, edited by Spiro, T.G. (Wiley, New York, 1981), pp. 291–358 and references therein.Google Scholar
7) Valentine, J.S and Mota de Freitas, D., J. Chem Ed. 62, 990 (1985).Google Scholar
8) Fee, J.A. and Gaber, B.P., J. Biol. Chem. 247, 60 (1972).CrossRefGoogle Scholar
9) Riflind, J.M, Inorganic Biochemistry. vol. I edited by Eichhorn, G.L. (Elsevier Scientific Publishing, New York, 1973) pp. 832–901 and references therein.Google Scholar
10) Sage, J.T., Morikis, D. and Champion, P.M., Biochem. 30, 1227 (1991).Google Scholar
11) Trinder, P., Ann. Clin. Biochem. 624 (1969).Google Scholar
12) Worthington, C.S. and Teller, J.D., Worthington Enzyme Manual (Freehold, NJ, 1972), p. 43.Google Scholar