Enzymatic hydrogen production: Conversion of renewable resources for energy production

被引:24
作者
Woodward, J [1 ]
Cordray, KA [1 ]
Edmonston, RJ [1 ]
Blanco-Rivera, M [1 ]
Mattingly, SM [1 ]
Evans, BR [1 ]
机构
[1] Oak Ridge Natl Lab, Div Chem Technol, Oak Ridge, TN 37831 USA
关键词
D O I
10.1021/ef990126l
中图分类号
TE [石油、天然气工业]; TK [能源与动力工程];
学科分类号
0807 ; 0820 ;
摘要
Using the enzymes glucose dehydrogenase (GDH) and hydrogenase, we have shown that a variety of sugars that are components of renewable resources can be enzymatically converted to molecular hydrogen. The rates at which hydrogen was evolved paralleled the substrate specificity of GDH. The highest rate of hydrogen production measured was 97.8 mu mol/h, and the stoichiometric yield of hydrogen was 98% with 50 mM glucose as the substrate. Lactose, sucrose, cellulose, xylan, steam-exploded aspen wood, and starch also served as substrates for hydrogen production when the corresponding enzymes were included in the reaction mixture to generate the appropriate monosaccharide for which GDH has specificity. The data obtained are discussed in the context of the rate-limiting steps of hydrogen production from renewable sugar and the possible applications of enzymatic hydrogen production.
引用
收藏
页码:197 / 201
页数:5
相关论文
共 14 条
[1]   Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterisation and N-terminal sequence [J].
Bonete, MJ ;
Pire, C ;
LLorca, FI ;
Camacho, ML .
FEBS LETTERS, 1996, 383 (03) :227-229
[2]  
Cowling ES, 1976, BIOTECHNOL BIOENG S, V6, P95
[3]   ENHANCED HYDROLYSIS OF SOLUBLE CELLULOSIC SUBSTRATES BY A METALLOCELLULASE WITH VERATRYL ALCOHOL-OXIDASE ACTIVITY [J].
EVANS, BR ;
MARGALIT, R ;
WOODWARD, J .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 1995, 51-2 :225-239
[4]  
Godfrey T, 1996, IND ENZYMOLOGY
[5]  
GREENBAUM E, 1984, PHOTOBIOCH PHOTOBIOP, V8, P323
[6]  
KOSTANTINIDIS K, 1993, BIOCHEM J, V291, P883
[7]   Thermophilic Fe(III)-reducing bacteria from the deep subsurface: The evolutionary implications [J].
Liu, SV ;
Zhou, JZ ;
Zhang, CL ;
Cole, DR ;
GajdarziskaJosifovska, M ;
Phelps, TJ .
SCIENCE, 1997, 277 (5329) :1106-1109
[8]  
MA KS, 1994, FEMS MICROBIOL LETT, V122, P245, DOI 10.1111/j.1574-6968.1994.tb07175.x
[9]   KINETIC-STUDIES OF THE ACTIVE-SITES FUNCTIONING IN THE QUINOHEMOPROTEIN FRUCTOSE DEHYDROGENASE [J].
MARCINKEVICIENE, J ;
JOHANSSON, G .
FEBS LETTERS, 1993, 318 (01) :23-26
[10]   PREPARATIVE PURIFICATION OF TRICHODERMA-REESEI NATIVE AND CORE CELLOBIOHYDROLASE-I BY ELECTROPHORESIS AND CHROMATOFOCUSING [J].
OFFORD, DA ;
LEE, NE ;
WOODWARD, J .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 1991, 28-9 :377-386