Remarkable thermostability of bioelectrodes based on enzymes immobilized within hydrophobic semi-solid matrices

Biotechnology and Applied Biochemistry

Volumn 30, Issue 2, 1999, Pages 177-183

  Liu, Jie ^a   Wang, Joseph ^b  

^a NANTONG MEDICAL COLLEGE   (China)

^b NEW MEXICO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL OXIDASE; AMINO ACID OXIDASE; CARBON; CATECHOL OXIDASE; GLUCOSE OXIDASE; LACTATE 2 MONOOXYGENASE; PEROXIDASE; RHODIUM;

ARTICLE; BIOSENSOR; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME ELECTRODE; ENZYME IMMOBILIZATION; HYDROPHOBICITY; TEMPERATURE; THERMOSTABILITY; TIME;

EID: 0032859199     PISSN: 08854513     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (30)

1. Jina, A. N. and Tierney, M. J. (1993) in Diagnostics in the Year 2000: Antibody, Biosensor and Nucleic Acid Technologies, chapter 19 (Singh, P., Sharma, B. P. and Tyle, P., eds.), pp. 343-365, Van Nastrand Reinhold, New York
2. Guilbault, G. G., Kauffmann, J. M. and Patriarche, G. J. (1991) Bioprocess Technol. 14, 209-262
3. Gupta, M. N. (ed.) (1993) Thermostability of Enzymes, Narosa, New Delhi
4. Gianfreda, L. and Scarfi, M. R. (1991) Mol. Cell. Biochem. 100, 97-128
5. Klibanov, A. M. (1983) Adv. Appl. Microbiol. 29, 1-28
6. Martinek, K and Berezin, I. V. (1977) J. Solid-Phase Biochem. 2, 343-385
7. Schulz, G. E. and Schirmer, R. H. (1979) Principles of Protein Structure, chapter 3, pp. 27-45, Springer Verlag, Berlin
8. Freeman, A. (1984) Trends Biotechnol. 2, 147-148
9. Gupta, M. N. (1992) Eur. J. Biochem. 203, 25-32
10. Gupta, M. N. (1991) Biotechnol. Appl. Biochem. 14, 1-11
11. Klibanov, A. M. (1989) Trends Biochem. Sci. 14, 141-144
12. Klibanov, A. M. (1986) Chemtech 16, 354-359
13. Wong, C. H. (1989) Science 244, 1145-1152
14. Zaks, A. and Klibanov, A. M. (1984) Science 224, 1249-1251
15. Wheeler, C. J. and Croteau, R. (1986) Arch. Biochem. Biophys. 248, 429-434
16. Klibanov, A. M. and Ahem, T. J. (1987) in Protein Engineering (Oxender, D. L. and Fox, C. F., eds.), pp. 213-218, Alan R. Liss, New York
17. Zaks, A. and Klibanov, A. M. (1988) J. Biol. Chem. 263, 3194-3201
18. Ayala, G., Tuena de GomoZ-Puyou, M., Gomez-Puyou, A. and Darszon, A. (1986) FEBS Lett. 203, 41-43
19. Garza-Ramos, G., Darszon, A., Tuena de GomoZ-Puyou, M. and Gomez-Puyou, A. (1990) Biochemistry 29, 751-757
20. Zaborsky, O. R. (1973) Immobilized Enzymes, CRC Press, Cleveland
21. Bowers, L. and Carr, P. (1976) Anal. Chem. 48, 544A-559A
22. Wang, J. and Lin, M. S. (1988) Anal. Chem. 60, 1545-1548
23. Gorton, L. (1995) Electroanalysis 7, 23-45
24. Amine, A. and Kauffmann, J. M. (1992) Bioelectrochem. Bioenerg. 28, 117-125
25. Connor, M., Sanchez, J., Wang, J., Smyth, M. R. and Mannino, S. (1989) Analyst 114, 1427-1429
26. Wang, J., Liu, J., Chen, L. and Lu, F. (1994) Anal. Chem. 66, 3600-3603
27. Fortier, G. and Belanger, D. (1991) Biotech. Bioeng. 37, 854-858
28. Sasso, S. V., Pierce, R. J., Walla, R. J. and Yacynych, A. M. (1990) Anal. Chem. 62, 1111-1117
29. Wang, J., Rivas, G. and Chicharo, M. (1996) Electroanalysis 8, 434-437
30. McReynolds, W. O. (1970) J. Chromatogr. Sci. 8, 685-691