Banta:Gels

Protein-based Hydrogels for Bioelectrocatalysis

Self-assembly is an essential process for all forms of life. For example, proteins spontaneously fold into well-defined 3-dimensional structures, and cellular organelles form that spatially segregate diverse cellular processes. As engineers aim to create new devices and systems at ever decreasing size scales, self-assembly processes become increaseingly attactive techniques.

We are collaborating with Plamen Atanassov at University of New Mexico, Scott Calabrese-Barton at Michigan State University and Shelley Minteer at Saint Louis University to make improved electrodes for biofuel cells. In a biofuel cell, redox enzymes are immobilized on electrode surfaces. Enzymes located at the anode are able to oxidize substrates and the electrons move through an external circuit to create power. On the cathode, other redox enzymes are able to use the electrons to reduce oxygen to water. The net result of this process is the generation of electricity from a variety of readily available biofuel sources, with oxygen as the terminal electron acceptor.

The architecture of the electrodes is crucial for biofuel cell performance. The enzymes on the electrodes must be positioned so that electrons can easily move between the enzymatic active site and the electorde surface (Direct Electron Transfer (DET)). Alternatively, the enzymes can be immoblilized with redox mediators, such as osmium, that facilitate the transport of electrons from the electrodes to the enzymes (Fig. 1). In this Mediated Electron Transport (MET) configuration, the enzyme and mediators are immobilized in a polymer matrix on the electrode surface. While this system has been used to demonstrate impressive biofuel cell performances, it is potentially hampered by poor dispersion of the enzyme and mediator within the polymer matrix, and complex manufacturing requirments.

We are using biological self-assembly to improve the biofuel cell electrode construction and performance (Fig. 2). Instead of combing enzymes and mediators in a polymer matrix, we are creating self-assembling protein-based hydrogels that intrinsically include the redox enzymes and the mediators. In this configuration the loading of the enzyme and the mediators into the hydrogel can be finely controlled, and the hydrogel assembly process will be well-defined and repeatable. These new bioelectrocatalytic hydrogels will have the potential to significantly improve biofuel cell performance.

Related Publications

1. Simon MJ, Gao S, Kang WH, Banta S, and Morrison B 3rd. TAT-mediated intracellular protein delivery to primary brain cells is dependent on glycosaminoglycan expression. Biotechnol Bioeng. 2009 Sep 1;104(1):10-9. DOI:10.1002/bit.22377 |
2. Chockalingam K, Lu HD, and Banta S. Development of a bacteriophage-based system for the selection of structured peptides. Anal Biochem. 2009 May 1;388(1):122-7. DOI:10.1016/j.ab.2009.01.042 |
3. Gao S, Simon MJ, Morrison B 3rd, and Banta S. Bifunctional chimeric fusion proteins engineered for DNA delivery: optimization of the protein to DNA ratio. Biochim Biophys Acta. 2009 Mar;1790(3):198-207. DOI:10.1016/j.bbagen.2009.01.001 |
4. Glykys DJ and Banta S. Metabolic control analysis of an enzymatic biofuel cell. Biotechnol Bioeng. 2009 Apr 15;102(6):1624-35. DOI:10.1002/bit.22199 |
5. Chen XJ, West AC, Cropek DM, and Banta S. Detection of the superoxide radical anion using various alkanethiol monolayers and immobilized cytochrome c. Anal Chem. 2008 Dec 15;80(24):9622-9. DOI:10.1021/ac800796b |
6. Wheeldon IR, Gallaway JW, Barton SC, and Banta S. Bioelectrocatalytic hydrogels from electron-conducting metallopolypeptides coassembled with bifunctional enzymatic building blocks. Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15275-80. DOI:10.1073/pnas.0805249105 |
7. Casali M, Banta S, Zambonelli C, Megeed Z, and Yarmush ML. Site-directed mutagenesis of the hinge peptide from the hemagglutinin protein: enhancement of the pH-responsive conformational change. Protein Eng Des Sel. 2008 Jun;21(6):395-404. DOI:10.1093/protein/gzn018 |
8. Blenner MA and Banta S. Characterization of the 4D5Flu single-chain antibody with a stimulus-responsive elastin-like peptide linker: a potential reporter of peptide linker conformation. Protein Sci. 2008 Mar;17(3):527-36. DOI:10.1110/ps.073257308 |
9. Gallaway J, Wheeldon I, Rincon R, Atanassov P, Banta S, and Barton SC. Oxygen-reducing enzyme cathodes produced from SLAC, a small laccase from Streptomyces coelicolor. Biosens Bioelectron. 2008 Mar 14;23(8):1229-35. DOI:10.1016/j.bios.2007.11.004 |
10. Wheeldon IR, Barton SC, and Banta S. Bioactive proteinaceous hydrogels from designed bifunctional building blocks. Biomacromolecules. 2007 Oct;8(10):2990-4. DOI:10.1021/bm700858p |
11. Chockalingam K, Blenner M, and Banta S. Design and application of stimulus-responsive peptide systems. Protein Eng Des Sel. 2007 Apr;20(4):155-61. DOI:10.1093/protein/gzm008 |
12. Banta S, Megeed Z, Casali M, Rege K, and Yarmush ML. Engineering protein and peptide building blocks for nanotechnology. J Nanosci Nanotechnol. 2007 Feb;7(2):387-401. DOI:10.1166/jnn.2007.153 |
13. Banta S, Vemula M, Yokoyama T, Jayaraman A, Berthiaume F, and Yarmush ML. Contribution of gene expression to metabolic fluxes in hypermetabolic livers induced through burn injury and cecal ligation and puncture in rats. Biotechnol Bioeng. 2007 May 1;97(1):118-37. DOI:10.1002/bit.21200 |
14. Banta S, Yokoyama T, Berthiaume F, and Yarmush ML. Effects of dehydroepiandrosterone administration on rat hepatic metabolism following thermal injury. J Surg Res. 2005 Aug;127(2):93-105. DOI:10.1016/j.jss.2005.01.001 |
15. Yokoyama T, Banta S, Berthiaume F, Nagrath D, Tompkins RG, and Yarmush ML. Evolution of intrahepatic carbon, nitrogen, and energy metabolism in a D-galactosamine-induced rat liver failure model. Metab Eng. 2005 Mar;7(2):88-103. DOI:10.1016/j.ymben.2004.09.003 |
16. Banta S, Yokoyama T, Berthiaume F, and Yarmush ML. Quantitative effects of thermal injury and insulin on the metabolism of the skeletal muscle using the perfused rat hindquarter preparation. Biotechnol Bioeng. 2004 Dec 5;88(5):613-29. DOI:10.1002/bit.20258 |
17. Sanli G, Banta S, Anderson S, and Blaber M. Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Sci. 2004 Feb;13(2):504-12. DOI:10.1110/ps.03450704 |
18. Yarmush ML and Banta S. Metabolic engineering: advances in modeling and intervention in health and disease. Annu Rev Biomed Eng. 2003;5:349-81. DOI:10.1146/annurev.bioeng.5.031003.163247 |
19. Banta S, Boston M, Jarnagin A, and Anderson S. Mathematical modeling of in vitro enzymatic production of 2-Keto-L-gulonic acid using NAD(H) or NADP(H) as cofactors. Metab Eng. 2002 Oct;4(4):273-84. DOI:10.1006/mben.2002.0231 |
20. Banta S and Anderson S. Verification of a novel NADH-binding motif: combinatorial mutagenesis of three amino acids in the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase. J Mol Evol. 2002 Dec;55(6):623-31. DOI:10.1007/s00239-002-2345-x |
21. Banta S, Swanson BA, Wu S, Jarnagin A, and Anderson S. Optimizing an artificial metabolic pathway: engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis. Biochemistry. 2002 May 21;41(20):6226-36. DOI:10.1021/bi015987b |
22. Banta S, Swanson BA, Wu S, Jarnagin A, and Anderson S. Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A. Protein Eng. 2002 Feb;15(2):131-40. DOI:10.1093/protein/15.2.131 |