효소연료전지의 Anode 제조조건이 OCV에 미치는 영향

김영숙; 이세훈; 추천호; 나일채; 이호; 박권필; Young-Sook Kim; Se-Hoon Lee; Cheun-Ho Chu; Il-Chai Na; Ho Lee; Kwon-Pil Park

Korean Chemical Engineering Research, Vol.53, No.1, 6-10, February, 2015

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효소연료전지의 Anode 제조조건이 OCV에 미치는 영향

Effect of Fabrication Method of Anode on OCV in Enzyme Fuel Cells

김영숙, 이세훈¹, 추천호, 나일채², 이호², 박권필 ^{1, †}

(주)ETIS, 415-813 경기도 김포시 고천읍 풍곡리 431-1
¹순천대학교 화학공학과, 540-742 전남 순천시 매곡동 315
²(주)CNL Energy, 540-742 전남 순천시 매곡동 315

Young-Sook Kim, Se-Hoon Lee¹, Cheun-Ho Chu, Il-Chai Na², Ho Lee², and Kwon-Pil Park^{1, †}

ETIS Co, 431-1 Punggok-ri, Gochon-eup, Gimpo-si, Gyeonggi 415-813, Korea
¹Department of Chemical Engineering, Sunchon National University, 315 Maegok-dong, Suncheon-si, Jeonnam 540-742, Korea
²CNL Energy Co, 315 Maegok-dong, Suncheon-si, Jeonnam 540-742, Korea

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초록

효소 전극 anode와 PEMFC용 전극 cathode를 이용하여 효소연료전지를 구동하였다. 효소 anode는 그래파이트 분말과 효소로서 글루코스 산화제, 전자매개체로서 페로센을 혼합해 압축해서 만들고 Nafion 이오노머로 코팅하였다. anode 제조조건을 변화시키며 OCV를 측정해 효소 anode 제조 최적조건을 찾았다. 효소 anode 압축 시 최적 압력은 9.0MPa였다. 효소 anode에서 그래파이트가 60%일 때 최고의 OCV를 나타냈다. anode 기질 용액의 최적 글루코스 농도는 1.7 mol/l이었으며, anode의 효소 활성은 7일 동안 안정적으로 유지되었다.

Enzyme fuel cells were composed of enzyme anode and PEMFC cathode. Enzyme anodes was fabricated by compression of a mixture of graphite particle, glucose oxidase as a enzyme and ferrocene as a mediator, and then coated with Nafion ionomer. Open circuit voltage (OCV) were measured with variation of anode manufacture factors, to find optimum condition of enzyme anode. Optimum pressure was 9.0 MPar for enzyme anode pressing process. Highest OCV was obtained at 60% graphite composition in enzyme anode. Optimum glucose concentration was 1.7mol/l in anode substrate solution and enzyme activity of anode was stable for 7 days.

Keywords:Enzyme Fuel Cells;OCV;Pressing Anode;Fabrication Method;Glucose Oxidase

[References]

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[1] Heller A, Phys. Chem. Chem. Phys., 6, 209 (2004)

[2] Mano N, Mao F, Heller A, J. Am. Chem. Soc., 125(21), 6588 (2003)

[3] Mano N, Mao F, Heller A, J. Am. Chem. Soc., 124(44), 12962 (2002)

[4] Mano N, Mao F, Shin W, Chen T, Heller A, Chem. Commun., 518 (2003)

[5] Leech D, Kavanagh P, Schuhmann W, Electrochim. Acta, 84, 223 (2012)

[6] Yuhashi N, Tomiyama M, Okuda J, Igarashi S, Ikebukuro K, Sode K, Biosens. Bioelectron., 20, 2145 (2005)

[7] Jenkins P, Tuurala S, Vaari A, Valkiainen M, Smolander M, Leech D, Enzyme Microb. Technol., 50(3), 181 (2012)

[8] Tsujimura S, Kano K, Ikeda T, Electrochemistry, 70, 940 (2002)

[9] Sato F, Togo M, Islam MK, Matsue T, Kosuge J, Fukasaku N, Kurosawa S, Nishizawa M, Electrochem. Commun., 7, 643 (2005)

[10] Kim H, Lee I, Kwon Y, Kim B, Ha S, Lee J, Kim J, Biosens. Bioelectron., 26, 3908 (2011)

[11] Cosnier S, Shan D, Ding SN, Electrochem. Commun., 12, 266 (2010)

[12] Zebda A, Gondran C, Cinquin P, Consier S, Sens. Actuators B-Chem., 173, 760 (2012)

[13] Bergmeyer HU, Gawehn K, Grassl M, “Methods of Enzyme Analysis,” second ed., Academic Press Inc., New York (1974)

[14] Song J, Woo M, Kim S, Ahn B, Lim T, Park K, Korean Chem. Eng. Res., 50(2), 187 (2012)

[15] Lee H, Kim T, Sim W, Kim S, Ahn B, Lim T, Park K, Korean J. Chem. Eng., 28(2), 487 (2011)