• Korean Chemical Engineering Research
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• 제60권4호
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• pp.550-556
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• 2022

당, 알코올, 유기산 및 아미노산 등과 같은 다양한 유기물에 포함된 화학에너지를 전기에너지로 전환시키는 효소 연료전지의 성능은 anode 뿐만 아니라 cathode에도 큰 영향을 받는다. 본 연구의 목적은 laccase 기반의 고성능 cathode 전극을 개발하는데 있다. 효소, 전자전달체 및 탄소나노튜브로 구성된 효소 복합체를 제조하고 이를 전극 표면에 다층으로 부착하며 층수 및 탄소나노튜브의 첨가 유무가 전극 성능에 미치는 영향을 조사하였다. 전극 표면에 효소-전자전달체(Lac-(PVI-Os-dCl))의 층수가 증가할수록 전극에서 발생되는 환원 전류량이 증가하였다. 탄소나노튜브가 첨가된 효소-전자전달체 복합체 전극(Lac-SWCNTs-(PVI-Os-dCl))이 Lac-(PVI-Os-dCl) 전극에 비하여 1.7배 많은 환원 전류를 생성하였다. Lac-SWCNTs-(PVI-Os-dCl)과 Lac-(PVI-Os-dCl)의 비율을 변화시키며 적층한 전극들에서 2층의 Lac-(PVI-Os-dCl)과 2층의 Lac-SWCNTs-(PVI-Os-dCl)으로 구성된 전극이 가장 많은 양의 환원 전류(10.1±0.1 µA)를 생성하였다. 단일 층의 Lac-(PVI-Os-dCl)로 구성된 cathode를 사용하는 셀과 최적화된 cathode를 사용하는 셀의 최대 생산 전력밀도는 각각 0.46±0.05와 1.23±0.04 µW/cm²였다. 본 연구 결과는 전극 표면에 laccase, 전자전달체 및 탄소나노튜브로 구성된 복합체의 적층 최적화를 통해 cathode 및 이를 이용하는 효소 연료전지의 성능을 향상시킬 수 있음을 시사한다.

• Bulletin of the Korean Chemical Society
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• 제25권8호
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• pp.1195-1201
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• 2004

Tyrosinase was covalently immobilized on platinum electrode according to the method we developed for laccase (Bull. Korean Chem. Soc. 2002, 23(7), 385) and p-chlorophenol, p-cresol, and phenol could be detected with sensitivities of 334, 139 and 122 nA/ ${\mu}M$ and the detection limits of 1.0, 2.0, and 2.5 ${\mu}M$, respectively. The response time ($t_{90\%}$) is 3 seconds for p-chlorophenol, and 5 seconds for p-cresol and phenol. The optimal pHs of the sensor are in the range of 5.0- 6.0. This sensor can tolerate at least 500 times repeated injections of p-chlorophenol with retaining 80% of initial activity. In case of tyrosinase and laccase co immobilized platinum electrode, the sensitivities are 560 nA/ ${\mu}M$ for p-phenylenediamine (PPD) and 195 nA/ ${\mu}M$ for p-chlorophenol, respectively. The sensitivity of the bi-enzyme sensor for PPD increases 70% compared to that of only laccase immobilized one, but the sensitivity for p-chlorophenol decreases 40% compared to that of only tyrosinase immobilized one. The sensitivity increase for the bi-enzyme sensor for PPD can be ascribed to the additional catalytic function of the co-immobilized tyrosinase. The sensitivity decrease for p-chlorophenol can be explained by the “blocking effect” of the co-immobilized laccase, which hinders the mass transport through the immobilized layer. If PPD was detected with the electrode that had been used for p-chlorophenol, the sensitivity decreased 20% compared to that of the electrode that had been used only for PPD. Similarly, if p-chlorophenol was detected with PPD detected electrode, the sensitivity also decreased 20%. The substrate-induced conformation changes of the enzymes in a confined layer may be responsible for the phenomena.

• 분석과학
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• 제27권4호
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• pp.181-186
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• 2014

• 한국전기전자재료학회:학술대회논문집
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• 한국전기전자재료학회 2000년도 영호남학술대회 논문집
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• pp.316-319
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• 2000

In the case of immobilizing of glucose oxidase into polypyrrole (PPy) using electrosynthesis, the glucose oxidase (GOx) forms a coordinate bond with the polymer's backbone. However, because of intrinsic insulation and net-chain of the enzyme, the charge transfer and mass transport are obstructed during the film growth. Therefore, the film growth is dull. We synthesized the enzyme electrode by electropolymerization added some organic solvent, A formative seeds of film growth is delayed by adding the solvent. The delay is induced by radical transfer between the solvent and pyrrole monomer. In the case of adding ethanol, the radical transfer shares the contribution of dopant between electrolyte anion and GOx polyanion. This may lead to increase amount of immobilized the enzyme in ppy. However, adding tetrahydrofuran (THF), the radical transfer is more brisk, resulting in short chained polymer. Therefore, the doping level is lowered and then amount of immobilized of enzyme is decreased. For the UV absorption spectra of synthetic solution before synthesis and after, in the case of ethanol added, the optical density was slightly decreased for the GOx peaks. It suggests amount of GOx in the solution was decreased and amount of GOx in the film was increased. We established qualitatively that amount of immobilization can be improved by adding a little ethanol in the synthetic solution. It is due to radical transfer reaction. The radical transfer shares the contribution of dopant between small and fast electrolyte anion and big and slow GOx polyanion.

• 분석과학
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• 제7권2호
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• pp.149-153
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• 1994

Squash-조직을 graphite rod disk 전극에 고정하여 메탄올 용매 속에서 L-ascorbic acid(AA)를 정량할 수 있는 전류법 바이오센서를 만들었다. 전극의 검출한계는 $2{\times}10^{-6}M$이었다. 순수한 ascorbate oxidase(AO)를 고정시켜 만든 전극에 비해 식물 조직에 들어 있는 효소로 만든 이 전극은 생촉매의 활성도가 높고 안정성이 좋았으며(1주간) 대단히 값싸게 만들 수 있었다.

• Journal of Microbiology and Biotechnology
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• 제16권4호
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• pp.505-510
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• 2006

A gallocyanine-bound nanoporous titanium dioxide electrode system was investigated to carry out a mediated enzyme reaction. Gallocyanine was bound either directly or through an aminopropylsilane linker to the film of nanoporous titanium dioxide and used as a mediator for nitrate reductase in the mediated enzymatic nitrate reduction. The electrode with the aminopropylsilane linker showed 20% higher efficiency of electron transfer at the same potential than that directly linked. The prepared electrodes showed $0.26{\mu}mol/h$ nitrate reduction at a $100mm^2$ surface of the electrode, and linear current response on nitrate ion concentration up to 1.0 mM, which is very useful as a biosensor of nitrate ion in water.

• Elastomers and Composites
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• 제41권4호
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• pp.231-237
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• 2006

부틸고무를 결합재로 사용하여 과산화수소 정량 바이오센서를 제작하고, 그것의 전기화학적 특성과 실용화 가능성을 살펴보았다. 전극은 본 실험실에서 연구되었던 실리콘 오일을 결합재로 사용한 동식물조직 바이오센서보다 수백 배 이상 큰 신호를 보여주었으며, $0.0{\sim}-1.00\;V$(vs. Ag/AgCl)의 넓은 퍼텐셜 영역에서 안정적으로 작동될 수 있었다. 또 신호전류는 실험 퍼텔셜 영역에서 전극전위에 따라 좋은 직선성을 보였다. 검출한계는 $3.0{\times}10^{-4}\;M$ 이었으며, Lineweaver-Burk 도시의 직선성은 효소가 전극 표면에 효과적으로 고정되어 있음을 확인시켜 주었다. 높은 감도에 의한 신호전류의 재현성과, 부틸고무의 결합력에 의한 전극물질의 기계적 안정성은 전극의 실용화 가능성을 보여 주었다.

• 동아시아식생활학회지
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• 제21권5호
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• pp.731-738
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• 2011

콜레스테롤의 신속하고 정확한 새로운 분석방법을 모색하기 위하여 본 연구에서는 전기적 전도성이 우수한 MWCNT를 이용하여 전극을 제작하였고, 여러 가지 효소고정화 방법을 통해 전기화학적 감응도 분석을 실시하였다. MWCNT의 전도성을 향상시키기 위해 아민기를 도입한 MWCNT-$NH_2$를 제조하였고, MWCNT-$NH_2$/GCE에 PB를 점착하여 작업전극을 제조하였다. 제조한 작업전극은 0.5~500 ${\mu}M$ $H_2O_2$ 농도 범위에서 농도가 증가함에 따라 전류가 비례적으로 증가하였고, 검출한계는 0.1 ${\mu}M$로 나타나 전극이 높은 감도를 가지고 있음을 확인하였다. 또한 콜레스테롤 검출을 위해 적합한 효소 반응기를 제작하기 위해 담체인 aminopropyl glass beads, CNBr-activated sepharose, Na-alginate, toyopearl beads에 cholesterol oxidase를 고정화시켜 바이오센서의 콜레스테롤 표준용액에 대한 감응도를 측정한 결과, aminopropyl glass beads과 CNBr-activated sepharose는 1~100 ${\mu}M$ 범위에서 선형관계를 보였으며, Na-alginate는 5~50 ${\mu}M$의 범위에서, toyopearl beads는 1~50 ${\mu}M$ 범위에서 선형관계를 나타내었다. 검출한계는 제작된 효소반응기 모두 1 ${\mu}M$로 나타나 콜레스테롤에 대한 높은 검출력을 보여주었으나, 특히 CNBr-activated sepharose와 Na-alginate를 이용한 효소반응기가 높은 coupling efficiency와 감응도를 보여 콜레스테롤 검출을 위한 본 바이오 센서 시스템에 적합한 것으로 나타났다.

• 한국신재생에너지학회:학술대회논문집
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• 한국신재생에너지학회 2009년도 춘계학술대회 논문집
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• pp.749-752
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• 2009

Anodized tubular titania ($TiO_2$) electrodes (ATTEs) are prepared and used as both the photoanode and the cathode substrate in a photoelectrochemical system designed to split water into hydrogen with the assistance of an enzyme and an external bias (solar cell). In particular, the ATTE used as the cathode substrate for the immobilization of the enzyme is prepared by two methods; adsorption and crosslinking. Results show that the optimized amount of enzyme is 10.98 units for the slurried enzyme, 3.66 units for the adsorbed one and 7.32 units for the crosslinked one, and the corresponding hydrogen evolution rates are 33.04, 148.58, and 234.88 umol/hr, respectively. The immobilized enzyme, specifically the chemically crosslinked one, seems to be much superior to the slurried enzyme, due to the enhanced charge-transfer process that is caused by the lower electrical resistance between the enzyme and the ATTE. This results in a greater number of accepted electrons and a larger amount of enzymes able to deal with the electrons.

• Food Science and Biotechnology
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• 제14권6호
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• pp.743-746
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• 2005

A dipstick-type immunochemical biosensor for the detection of the organophosphorus insecticide fenthion was developed using a screen-printed electrode system as an amperometric transducer with polyclonal antibodies against fenthion as a bioreceptor. The assay of the biosensor involved competition between the pesticide in the sample and pesticide-glucose oxidase conjugate for binding to the antibody immobilized on the membrane. This was followed by measurement of the activity of the bound enzyme by the supply of the enzyme substrate (glucose) and amperometric determination of the enzyme reaction product ($H_2O_2$). The activity of the bound enzyme was inversely proportional to the concentration of pesticide. The optimized sensor system showed a linear response against the logarithm of the pesticide concentration ranging from $10^{-2}$ to $10^3\;{\mu}g/L$.