Immobilization and enzymatic properties of Bacillus megaterium glucose dehydrogenase
Abstract
The enzymatic production of hydrogen gas from renewable sources of energy; e.g., cellulose, starch, lactose, can be obtained by coupling the reactions catalyzed by glucose dehydrogenase (GDH) and hydrogenase. In order to enhance the thermostability of GDH from Bacillus megaterium, the enzyme was immobilized by ionic adsorption using the polycationic polymer DEAE-(dextran)Sephadex. The effect of enzyme concentration on immobilization showed a tendency to increase the activity of the immobilized enzyme with the increase of the amount of added GDH. When the enzyme: support ratio was 15.97 U: 100 mg, the immobilization yield was 84.76%. The enzymatic profiles for the immobilized GDH were a little different when compared to those for free enzyme with respect to the effects of pH and temperature. Concerning the effect of incubation time carried at pH 7.5 and at 40{degrees}C, the maximum production of reduced coenzyme by the immobilized enzyme was reached within 4 h and it was maintained up to 16 h without loss of enzymatic activity. The coupling of the immobilized GDH activity with that for free alkaline cellulose (Novozym. 342) demonstrated the possibility for obtaining reduced coenzyme from the cellulose hydrolysis and the immobilized GDH could be reassayed 10 times maintaining its enzymemore »
- Authors:
-
- Federal Univ. of Parana, Curitiba, PR (Brazil)
- Oak Ridge National Lab., TN (United States)
- Publication Date:
- OSTI Identifier:
- 478726
- Report Number(s):
- CONF-960958-
TRN: 97:002640-0118
- DOE Contract Number:
- AC05-96OR22464
- Resource Type:
- Conference
- Resource Relation:
- Conference: Partnerships to develop and apply biomass technologies, Nashville, TN (United States), 15-19 Sep 1996; Other Information: PBD: 1996; Related Information: Is Part Of Bioenergy `96: Partnerships to develop and apply biomass technologies. Volume I and II; PB: 1171 p.
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 08 HYDROGEN FUEL; 09 BIOMASS FUELS; OXIDOREDUCTASES; ENZYME ACTIVITY; IMMOBILIZED ENZYMES; HYDROGEN PRODUCTION; BACILLUS MEGATERIUM
Citation Formats
Baron, M, Fontana, J D, Guimaraes, M F, and Woodward, J. Immobilization and enzymatic properties of Bacillus megaterium glucose dehydrogenase. United States: N. p., 1996.
Web.
Baron, M, Fontana, J D, Guimaraes, M F, & Woodward, J. Immobilization and enzymatic properties of Bacillus megaterium glucose dehydrogenase. United States.
Baron, M, Fontana, J D, Guimaraes, M F, and Woodward, J. 1996.
"Immobilization and enzymatic properties of Bacillus megaterium glucose dehydrogenase". United States.
@article{osti_478726,
title = {Immobilization and enzymatic properties of Bacillus megaterium glucose dehydrogenase},
author = {Baron, M and Fontana, J D and Guimaraes, M F and Woodward, J},
abstractNote = {The enzymatic production of hydrogen gas from renewable sources of energy; e.g., cellulose, starch, lactose, can be obtained by coupling the reactions catalyzed by glucose dehydrogenase (GDH) and hydrogenase. In order to enhance the thermostability of GDH from Bacillus megaterium, the enzyme was immobilized by ionic adsorption using the polycationic polymer DEAE-(dextran)Sephadex. The effect of enzyme concentration on immobilization showed a tendency to increase the activity of the immobilized enzyme with the increase of the amount of added GDH. When the enzyme: support ratio was 15.97 U: 100 mg, the immobilization yield was 84.76%. The enzymatic profiles for the immobilized GDH were a little different when compared to those for free enzyme with respect to the effects of pH and temperature. Concerning the effect of incubation time carried at pH 7.5 and at 40{degrees}C, the maximum production of reduced coenzyme by the immobilized enzyme was reached within 4 h and it was maintained up to 16 h without loss of enzymatic activity. The coupling of the immobilized GDH activity with that for free alkaline cellulose (Novozym. 342) demonstrated the possibility for obtaining reduced coenzyme from the cellulose hydrolysis and the immobilized GDH could be reassayed 10 times maintaining its enzyme activity.},
doi = {},
url = {https://www.osti.gov/biblio/478726},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Dec 31 00:00:00 EST 1996},
month = {Tue Dec 31 00:00:00 EST 1996}
}