论文部分内容阅读
Tyrosinase(TYR) was covalently immobilized onto amino-functionalized carbon felt surface via glutaraldehyde-coupling under ultrasonic treatment for 10 min.The resulting TYR-immobilized carbon felt was used as a working electrode unit of bioelectrocatalytic flow-through detector for TYR substrates(catechol,p-chlorophenol(p-CP),p-cresol,phenol etc.).Cathodic peak currents based on the electroreduction of enzymatically produced o-quinones were detected at-50 mV vs.Ag/AgCl.Compared with previous work in which TYR was immobilized onto amino-functionalized carbon felt for 16 hr without the ultrasonic treatment,we succeeded in(1) shortening the enzyme immobilization time from 16 hr to 10 min,(2) enhancing the sensitivity of p-CP,and(3) improving the operational stability of p-CP.The ultrasonic treatment during the TYR immobilization step would lead to certain changes in the structure of the immobilized TYR and the morphology of the immobilized TYR-layer on the carbon felt surface.
Tyrosinase (TYR) was covalently immobilized onto glutaraldehyde-coupling under ultrasonic treatment for 10 min. The resulting TYR-immobilized carbon felt was used as a working electrode unit of bioelectrocatalytic flow-through detector for TYR substrates (catechol , p-chlorophenol (p-CP), p-cresol, phenol etc.). Cathodic peak currents based on the electroreduction of enzymatically produced o-quinones were detected at-50 mV vs. Ag / AgCl. Compared with previous work in which TYR was immobilized onto amino-functionalized carbon felt for 16 hr without the ultrasonic treatment, we succeeded in (1) shortening the enzyme immobilization time from 16 hr to 10 min, (2) enhancing the sensitivity of p-CP, and (3) improving the operational stability of p-CP. The ultrasonic treatment during the TYR immobilization step would lead to certain changes in the structure of the immobilized TYR and the morphology of the immobilized TYR-layer on the carbon felt surface.