By Topic

Conductivity-Based Catechol Sensor Using Tyrosinase Immobilized in Porous Silicon

Sign In

Cookies must be enabled to login.After enabling cookies , please use refresh or reload or ctrl+f5 on the browser for the login options.

Formats Non-Member Member
$31 $13
Learn how you can qualify for the best price for this item!
Become an IEEE Member or Subscribe to
IEEE Xplore for exclusive pricing!
close button

puzzle piece

IEEE membership options for an individual and IEEE Xplore subscriptions for an organization offer the most affordable access to essential journal articles, conference papers, standards, eBooks, and eLearning courses.

Learn more about:

IEEE membership

IEEE Xplore subscriptions

5 Author(s)
Tembe, S. ; Dept. of Chem., Bhabha Atomic Res. Centre, Mumbai ; Chaudhari, Prajakta S. ; Bhoraskar, S.V. ; D'Souza, S.F.
more authors

A conductivity-based catechol biosensor was developed using porous silicon as an immobilization matrix for enzyme tyrosinase. The enzyme was extracted from plant source Amorphophallus companulatus and immobilized in an electrochemically etched surface of p-type silicon. The presence of enzyme in a porous structure and the retention of enzyme activity were confirmed by scanning electron microscopy and spectrophotometric studies, respectively. The principle of the sensor is based on the change in the conductivity of the tyrosinase-entrapped porous silicon matrix. When the entrapped tyrosinase interacted with catechol, the change in the current voltage (I-V) characteristics was obtained, which was proportional to analyte concentration. The analytical characteristics of the sensor including response time, linearity range, lower detection limit, reusability, and storage stability were studied.

Published in:

Sensors Journal, IEEE  (Volume:8 ,  Issue: 9 )