Development of Convenient Vitamin C Sensor Using Cucumber Microtissue Adsorbed on a Porous Carbon Material

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  • TOMITA Ryoichi
    Department of Materials and Engineering, Graduate School of Engineering, Saitama Institute of Technology
  • KOKUBUN Kentaro
    Department of Applied Chemistry, Saitama Institute of Technology
  • NAKAZATO Seiko
    Department of Applied Chemistry, Saitama Institute of Technology
  • UCHIYAMA Shunichi
    Department of Materials and Engineering, Graduate School of Engineering, Saitama Institute of Technology

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Other Title
  • キュウリの微少組織を吸着固定した多孔性炭素材料を用いる簡易型ビタミンＣセンサーの開発
  • キュウリ ノ ビショウ ソシキ オ キュウチャク コテイ シタ タコウセイ タンソ ザイリョウ オ モチイル カンイガタ ビタミン Cセンサ ノ カイハツ

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Abstract

The utilization of biological tissues containing large amount of enzymes is effective for fabricating inexpensive enzyme sensors, but the lifetime of enzymes in a biological tissue is rather short due to its putrefaction compared with the enzyme sensors using an immobilized purified enzyme membrane. In this work, cucumber juice containing ascorbte oxidase (ASOD) was used to immobilize ASOD to a porous carbon material by adsorption; this modified carbon material was combined with an oxygen electrode to fabricate a L-ascorbic acid (AsA) sensor. We found that an excellent linear relationship between AsA concentration and current response was obtained, and the stability of the sensor response was longer than at least one month. The reason why the lifetime of the enzyme sensor increases is that the microdebris of tissue is confined into the micropores of the carbon fibers, and the leaking or unfolding of enzyme does not take place. The porous carbon material adsorbed by purified ASOD also showed a similar long lifetime and a chemically amplified response (detection limit was 2.0 × 10−8 M) was observed by 0.05 M dithiothreithol (DTT). However, in the case of a microtissue adsorbed carbon material, amplification of the sensor response using DTT was not observed, because the access of DTT to enzyme in tissue is difficult, differing from purified enzyme.<br>

Journal

  • BUNSEKI KAGAKU

    BUNSEKI KAGAKU 54 (9), 913-916, 2005

    The Japan Society for Analytical Chemistry

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