• 한국신재생에너지학회:학술대회논문집
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• 한국신재생에너지학회 2010년도 춘계학술대회 초록집
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• pp.227.2-227.2
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• 2010

본 연구에서는 양극산화된 $TiO_2$ 전극(anodized tubular $TiO_2$ electrode, ATTE)을 수소제조용 PEC(Photoelectrochemical)시스템에서 광어노드와 기존의 백금전극을 대체하고 $H^+$ 환원능을 향상시키기 위하여 엔자임(Pyrococcus furiosus, Pfu)을 고정화한 후 캐소드로 동시에 활용하였으며, 엔자임 고정을 위한 crosslinker 종류 및 금속담지 여부, ATTE 길이를 통한 수소발생양에 미치는 영향을 연구하였다. ATTE 표면과 엔자임의 amine group의 연결을 위하여 heterobifunctional crosslinker로써 사슬 길이가 상대적으로 짧은 Sulfo-SDA가 유리하였으며, 금속담지의 경우 짧은 튜브의 경우 1% 내에서 효과가 증진되었으나 긴 튜브의 경우는 오히려 광전류 및 궁극적으로 수소발생속도에 불리하게 작용하였다. 또한, 튜브 길이가 긴 ATTE가 짧은 ATTE 보다 수소발생양에서 더욱 효율적임을 알 수 있었다. 텅스텐산화물 담지의 가시광감응에의 담지 효과는 예비 실험 결과로 나타나지 않아, 추가적인 연구가 필요한 것으로 판단된다.

• 한국수소및신에너지학회논문집
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• 제33권5호
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• pp.507-514
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• 2022

There is growing interest in sustainable energy sources that can reduce fossil fuel dependence and environmental pollution while meeting rapidly growing energy demands. Hydrogen have been investigated as one of the ideal alternative energies because it has relatively high efficiency without emitting pollutants. The light-sensitized enzymatic (LSE) system, which uses hydrogenase-enzymes, is one of the methods towards economically feasible system configurations that enhance the rate of hydrogen generation. Hydrogenase is an enzyme that catalyzes a reversible reaction that oxidizes molecular hydrogen or produces molecular hydrogen from protons and electrons. In this paper, utilization of [NiFe]-hydrogenase (from Pyrococcus furiosus) in photoelectrochemical hydrogen production system such as handling, immobilization, physicochemical and electrochemical analysis, process parameters, etc. was introduced.

• 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.