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Biotechnology and Applied Biochemistry (1999) 30, (177–183) (Printed in Great Britain)

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

Jie Liu*¹ and Joseph Wang†

*Department of Chemistry, Nantong Medical College, Nantong, JS 226001, People's Republic of China, and †Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, NM 88003, U.S.A.

¹ To whom correspondence should be addressed.

An enhanced resistance to thermal denaturation was investigated for enzymes immobilized within hydrophobic semi-solid matrices compared with both free enzymes and polymer-entrapped enzymes. The bioelectrodes based on the immobilization of glucose oxidase, lactate oxidase, alcohol oxidase, polyphenol oxidase, peroxidase and L-amino acid oxidase within a carbon-paste matrix were constructed to examine their thermal stabilitiy at 60 °C or 80 °C. The rhodium/glucose oxidase-containing carbon-paste electrode was found to offer a remarkable stability when incubated at 60 °C over a long period of 4 months, with only a decrease of approx. 15% in activity. The comparative studies suggest that thermal stabilization established by this enzyme-immobilization procedure varies with the enzyme's inherent stability, the incubation temperature and the immobilizing reagent, such as pasting liquid.

Received 29 April 1999/28 June 1999; accepted 14 July 1999

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