Skip to main content Accessibility help

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

  • Stacey A. Yamanaka (a1), Lisa M. Ellerby (a1), Ester H. Lan (a2), Clinton R. Nishida (a1), Fumito Nishida (a2), Bruce Dunn (a2), Joan Selverstone Valentine (a1) and Jeffrey I. Zink (a1)...


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.



Hide All
1) Brinker, C.J. and Scherer, G., Sol-Gel Science: The Physics and Chemistry of Sol-Gel Processing (Academic Press, Boston, 1990).
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).
3) Braun, S., Rappoport, S., Zusman, R., Avnir, D., and Ottolenghi, M., Mater. Lett. 10, 1 (1990).
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. 255270.
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.
6) Valentine, J.S. and Pantoliano, M.W., Copper Proteins, edited by Spiro, T.G. (Wiley, New York, 1981), pp. 291358 and references therein.
7) Valentine, J.S and Mota de Freitas, D., J. Chem Ed. 62, 990 (1985).
8) Fee, J.A. and Gaber, B.P., J. Biol. Chem. 247, 60 (1972).
9) Riflind, J.M, Inorganic Biochemistry. vol. I edited by Eichhorn, G.L. (Elsevier Scientific Publishing, New York, 1973) pp. 832901 and references therein.
10) Sage, J.T., Morikis, D. and Champion, P.M., Biochem. 30, 1227 (1991).
11) Trinder, P., Ann. Clin. Biochem. 624 (1969).
12) Worthington, C.S. and Teller, J.D., Worthington Enzyme Manual (Freehold, NJ, 1972), p. 43.


Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed