Hostname: page-component-77c89778f8-fv566 Total loading time: 0 Render date: 2024-07-18T12:03:52.891Z Has data issue: false hasContentIssue false

Formation of composite gel fiber from cellulose acetate and zirconium tetra-n-butoxide and entrap-immobilization of β-galactosidase on the fiber

Published online by Cambridge University Press:  31 January 2011

K. Nakane*
Affiliation:
Department of Materials Science and Engineering, Faculty of Engineering, Fukui University, Bunkyo 3–9-1, Fukui 910–8507, Japan
T. Ogihara
Affiliation:
Department of Materials Science and Engineering, Faculty of Engineering, Fukui University, Bunkyo 3–9-1, Fukui 910–8507, Japan
N. Ogata
Affiliation:
Department of Materials Science and Engineering, Faculty of Engineering, Fukui University, Bunkyo 3–9-1, Fukui 910–8507, Japan
Y. Kurokawa
Affiliation:
Division of Materials Chemistry, Graduate School of Engineering, Tohoku University, Aramaki, Aoba-ku, Sendai 980–8579, Japan
*
a)Address all correspondence to this author. e-mail: nakane@matse.fukui-u.ac.jp
Get access

Abstract

The formation of a composite gel fiber from cellulose acetate and zirconium tetra-n-butoxide was examined. The gel was thought to have formed by the coordination of OH and CO groups of cellulose to zirconium, taking six coordination numbers around the zirconium. The gel fiber had good stability in common solvents, phosphate solution, and electrolyte solution. Then, under mild conditions, a β-galactosidase was entrap-immobilized on it. The apparent Michaelis constant of the Immobilized β-galactosidase was larger than that of native β-galactosidase, whereas the opposite tendency was observed for the maximum reaction velocity. The activity of the immobilized β-galactosidase increased as the fiber diameter decreased. These findings indicated that lactose hydrolysis took place in the vicinity of the fiber surface. The immobilized β-galactosidase had a higher thermal stability than the native type.

Type
Articles
Copyright
Copyright © Materials Research Society 2003

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

1.Wen, J. and Wilkes, G.L., Chem. Mater. 8, 1667 (1996).CrossRefGoogle Scholar
2.Immobilized Bio-Catalysis, edited by Chibata, I. (Kodansya, Tokyo, 1986, in Japanese).Google Scholar
3.Veliky, I.A. and Mclear, R.J.C., Immobilized Biosystems (Blakie Academic & Professional, New York, 1994).CrossRefGoogle Scholar
4.Nakane, K., Takahashi, K., Suzuki, F., and Kurokawa, Y., Sen’i Gakkaishi 55, 563 (1999).CrossRefGoogle Scholar
5.Nakane, K., Ogihara, T., Ogata, N., and Kurokawa, Y., J. Appl. Polym. Sci. 81, 2084 (2001).CrossRefGoogle Scholar
6.Ikeda, Y., Kurokawa, Y., Nakane, K., and Ogata, N., Cellulose, 9, 369 (2002).CrossRefGoogle Scholar
7.Rogalski, J., Dawidowicz, A., and Leonowics, A., J. Mol. Catal. 93, 233 (1994).CrossRefGoogle Scholar
8.Carrara, C.R. and Rubiolo, A.C., Chem. Eng. J. 65, 93 (1997).CrossRefGoogle Scholar
9.Liu, H., Li, H., Ying, T., Sun, K., Qin, Y., and Qi, D., Analy. Chim. Acta 358, 137 (1998).CrossRefGoogle Scholar
10.Jordão, R.B., Brandi, I.V., and Passos, F.M.L., J. Food Biochem. 25, 257 (2001).CrossRefGoogle Scholar
11.Zhou, Q.Z.K. and Chen, X.D., J. Food Eng. 48, 69 (2001).CrossRefGoogle Scholar
12.Filho, U.P.R., Gushikem, Y., Fujiwara, F.Y., Castro, S.C., Torriani, I.C.L., and Cavalcanti, L.P., Langmuir 10, 4357 (1994).CrossRefGoogle Scholar
13.Izumi, K., Murakami, M., Deguchi, T., Morita, A., Tohge, N., and Minami, T., J. Am. Ceram. Soc. 72, 1465 (1989).CrossRefGoogle Scholar