Biofuel cell controlled by enzyme logic network--approaching physiologically regulated devices.
A "smart" biofuel cell switchable ON and OFF upon application of several chemical signals processed by an enzyme logic network was designed. The biocomputing system performing logic operations on the input signals was composed of four enzymes: alcohol dehydrogenase (ADH), amyloglucosidase (AGS), invertase (INV) and glucose dehydrogenase (GDH). These enzymes were activated by different combinations of chemical input signals: NADH, acetaldehyde, maltose and sucrose. The sequence of biochemical reactions catalyzed by the enzymes models a logic network composed of concatenated AND/OR gates. Upon application of specific "successful" patterns of the chemical input signals, the cascade of biochemical reactions resulted in the formation of gluconic acid, thus producing acidic pH in the solution. This resulted in the activation of a pH-sensitive redox-polymer-modified cathode in the biofuel cell, thus, switching ON the entire cell and dramatically increasing its power output. Application of another chemical signal (urea in the presence of urease) resulted in the return to the initial neutral pH value, when the O(2)-reducing cathode and the entire cell are in the mute state. The reversible activation-inactivation of the biofuel cell was controlled by the enzymatic reactions logically processing a number of chemical input signals applied in different combinations. The studied biofuel cell exemplifies a new kind of bioelectronic device where the bioelectronic function is controlled by a biocomputing system. Such devices will provide a new dimension in bioelectronics and biocomputing benefiting from the integration of both concepts.
Department of Chemistry and Biomolecular Science, and NanoBio Laboratory (NABLAB), Clarkson University, Potsdam, NY 13699-5810, USA.
Tsz Kin
TK
Tam
Marcos
M
Pita
Maryna
M
Ornatska
Evgeny
E
Katz
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology; D055162:Biocatalysis; D001674:Bioelectric Energy Sources / Q000382:microbiology; D004563:Electrochemistry / Q000295:instrumentation*; D004566:Electrodes; D004798:Enzymes / Q000378:metabolism*; D005658:Fungi / Q000201:enzymology; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism; D005942:Gluconates / Q000378:metabolism; D005947:Glucose / Q000737:chemistry / Q000378:metabolism; D042843:Glucose 1-Dehydrogenase / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008128:Logic; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D043324:beta-Fructofuranosidase / Q000378:metabolism
D004798:Enzymes; D005942:Gluconates; D000426:Alcohol Dehydrogenase; D042843:Glucose 1-Dehydrogenase; D043324:beta-Fructofuranosidase; D005087:Glucan 1,4-alpha-Glucosidase; D005947:Glucose; C030691:gluconic acid