Journal
BIOELECTROCHEMISTRY
Volume 69, Issue 1, Pages 41-48Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2005.11.001
Keywords
tyrosinase; immobilization; poly(indole-5 carboxylic acid); Raman spectra
Ask authors/readers for more resources
A conducting, polymeric film of poly(indole-5 carboxylic acid) has been prepared by electrochemical polymerization for covalent immobilization of an enzyme belonging to the family of phenoloxidases-tyrosinase. The polymer was characterized by cyclic voltammetry, UV-VIS and Raman spectroscopy in a buffer solution. As the polymer contains pendant carboxylic groups one-step carbodiimide method was used to immobilize tyrosinase on the polymer matrix. Immobilization of tyrosinase was confirmed by surface enhanced resonance Raman scattering spectra (SERRS) and by cyclic voltammetry as well. Tyrosinase was shown to retain its biological activity when being immobilized on the polymer surface. As proved by the electrochemical and spectroelectrochemical (UV-VIS) experiments, tyrosinase covalently bonded to the polymer matrix effectively catalyzes oxidation of catechol. The reduction current of o-quinones was measured as a function of catechol 2 concentration. The linear dependence was found to be 15 mu M of catechol with sensitivity of 250 mA/M cm(2). (c) 2005 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available