Three-dimensional laccase electrodes for miniaturised fuel cell power sources
Lead Research Organisation:
University of Manchester
Department Name: Materials
Abstract
Laccase is a protein excreted by white-rot fungi that works as well or better than precious metals at catalysing the reduction of oxygen to water. This chemical reaction is central to almost all low-temperature fuel cells that work in air.Fuel cells are devices that convert chemical energy from a fuel like methanol or hydrogen directly and efficiently into electrical energy. In contrast, when fuel is burned in a generator, the fuel's chemical energy is converted into thermal energy (hot gases) and mechanical energy (moving pistons) before it becomes electrical energy. Each energy conversion step has losses from heat loss and friction and from inescapable inefficiencies governed by the laws of thermodynamics; fuel cells, on the other hand, can have greater efficiencies by bypassing these intermediate stages.In most fuel cells the oxygen reduction reaction takes place on the surface of particles of expensive precious metals (usually platinum). Laccase catalyses the same reaction using only four copper atoms per enzyme molecule. Laccase catalysis is more energetically efficient, nearly as rapid, and more selective against catalyst-killing gaseous impurities.There are two key problems with using laccase in fuel cells. The first is stability: enzymes are complex and often fragile biological polymers that need to be properly oriented to work in a fuel cell. However, I have developed a technique that extends the working lifetime of laccase in a fuel cell from hours to several months. The second is the amount of electric current that is generated from a given area or volume. The platinum surface can host thousands of reactions at once while the each laccase molecule can only react one oxygen molecule at a time. To compensate for this, I am proposing introducing laccase into porous, three-dimensional electrode materials, essentially taking laccase from working on a open plain and moving it to a multi-storey office complex. For laccase to function as efficiently as possible, it needs to have its reaction needs met: a good supply of oxygen (fast gas diffusion), a constant concentration of hydrogen ions (buffered pH), and a well-connected electrical supply. Designing and building this infrastructure requires a thorough understanding of the interactions between the enzyme's surface and the surface to which it is attached and careful control of how material flows through the pores. Extending the surfaces into the third dimension lets us make more compact power sources that are suitable, for example, for small electronics like portable music players and mobile phones.Most of the surface area of porous materials is on the inside of the structure and probing an interior surface is always a challenge. I will use small gaseous molecules explore the interior, high-energy beams of metal ions to cut open the structure, high-resolution electron microscopy to examine it, and electronic and spectroscopic methods that can interrogate the interaction between the enzyme and a surface.This work is supported by an active, ongoing collaboration with experts in fungal biology. They are currently working on understanding the molecular biology behind laccase, first to mass produce the enzyme, followed by genetic engineering to change laccase's catalytic behaviour, selectivity and surface interactions.In addition to portable fuel cells that work at ambient temperatures, we may also discover more efficient, less expensive catalysts and learn how enzymes are able to carry out the oxygen reduction reaction with copper, a common metal from the first row of the transition metals, rather than platinum, a rare and expensive metal from the third row.
Organisations
People |
ORCID iD |
Christopher Blanford (Principal Investigator) |
Publications
Blanford CF
(2013)
The birth of protein electrochemistry.
in Chemical communications (Cambridge, England)
Cracknell J
(2012)
Developing the mechanism of dioxygen reduction catalyzed by multicopper oxidases using protein film electrochemistry
in Chemical Science
McArdle T
(2015)
Optimizing the Mass-Specific Activity of Bilirubin Oxidase Adlayers through Combined Electrochemical Quartz Crystal Microbalance and Dual Polarization Interferometry Analyses.
in ACS applied materials & interfaces
McNamara TP
(2016)
A sensitivity metric and software to guide the analysis of soft films measured by a quartz crystal microbalance.
in The Analyst
Singh K
(2013)
Sources of activity loss in the fuel cell enzyme bilirubin oxidase
in Energy & Environmental Science
Description | In addition to discoveries noted in EP/G00434X/1, which is this grant before transferring to U. Manchester: 1. We found that there is a fundamental issue in the application of enzymes as fuel cell catalysts when they are directly immobilised on an electrode surface. Changing the driving force, equivalent to drawing variable amounts of current from a fuel cell, causes the enzymatic electrocatalyst to degrade much more rapidly than when used with a continual current load (minutes versus months). 2. We found that our technique for monitoring the efficient use of enzyme electrocatalysts has a lucrative application in industrial biotechnology: creating fine chemicals in through enzymatically catalysed chemical transformations. 3. We found evidence of two new enzymatic states that affect the short-term performance of technological devices based on multicopper oxidases. 4. We developed a new technique that combines electrochemistry and modelling to quantify the rates of all the sub-steps in enzymatically catalysed oxygen reduction. |
Exploitation Route | This will greatly affect the design of any fuel cells based on enzymes. Our method development should have an impact on aspects of industrial biotech in terms of more efficient enzyme use and in biosensor design, in terms of improving long-term performance, especially for those used for continuous monitoring. |
Sectors | Chemicals Energy Healthcare Pharmaceuticals and Medical Biotechnology |
Description | We trialled our enzyme electrodes on a commercial fuel cell rig with our industrial partner C-Tech in membrane-free alcohol oxidation fuel cells using nanoparticles from a Brazilian collaborator. |
First Year Of Impact | 2016 |
Sector | Energy |
Impact Types | Societal |
Description | ALERT14 |
Amount | £491,200 (GBP) |
Funding ID | BB/M011658/1 |
Organisation | Biotechnology and Biological Sciences Research Council (BBSRC) |
Sector | Public |
Country | United Kingdom |
Start | 05/2014 |
End | 07/2015 |
Description | BBSRC |
Amount | £354,495 (GBP) |
Funding ID | BB/M007316/1 |
Organisation | Biotechnology and Biological Sciences Research Council (BBSRC) |
Sector | Public |
Country | United Kingdom |
Start | 01/2015 |
End | 12/2017 |
Description | BBSRC IAA |
Amount | £11,817 (GBP) |
Organisation | Biotechnology and Biological Sciences Research Council (BBSRC) |
Sector | Public |
Country | United Kingdom |
Start | 08/2015 |
End | 07/2016 |
Description | DTA studentship |
Amount | £61,000 (GBP) |
Organisation | Higher Education Funding Council for England |
Sector | Public |
Country | United Kingdom |
Start | 09/2012 |
End | 04/2016 |
Description | Electricity generation from biofuels using hybrid inorganic-enzymatic fuel cells |
Amount | £44,367 (GBP) |
Funding ID | Internal: 111879 |
Organisation | Engineering and Physical Sciences Research Council (EPSRC) |
Sector | Public |
Country | United Kingdom |
Start | 08/2016 |
End | 03/2017 |
Description | Graphene Bioscience Interdisciplinary Grand Challenge |
Amount | £23,133 (GBP) |
Organisation | University of Manchester |
Sector | Academic/University |
Country | United Kingdom |
Start | 04/2013 |
End | 09/2013 |
Description | Graphene NowNano studentship |
Amount | £65,000 (GBP) |
Organisation | Imperial College London |
Department | EPSRC Centres for Doctoral Training |
Sector | Academic/University |
Country | United Kingdom |
Start | 09/2014 |
End | 09/2018 |
Description | Industrial applicability of blue multicopper oxidases to direct methanol fuel cells |
Amount | £10,000 (GBP) |
Funding ID | Project Ref: 111321 |
Organisation | Biotechnology and Biological Sciences Research Council (BBSRC) |
Sector | Public |
Country | United Kingdom |
Start | 08/2016 |
End | 02/2017 |
Description | Nownano DTP |
Amount | £74,000 (GBP) |
Organisation | Engineering and Physical Sciences Research Council (EPSRC) |
Sector | Public |
Country | United Kingdom |
Start | 09/2013 |
End | 09/2017 |
Description | Nownano DTP |
Amount | £74,000 (GBP) |
Organisation | Engineering and Physical Sciences Research Council (EPSRC) |
Sector | Public |
Country | United Kingdom |
Start | 09/2010 |
End | 09/2014 |
Description | Reynaud's & Scleroderma Association |
Amount | £111,268 (GBP) |
Organisation | Raynaud's & Scleroderma Association |
Sector | Charity/Non Profit |
Country | United Kingdom |
Start | 07/2015 |
End | 07/2017 |
Title | Method for modelling multicopper oxidase electrochemistry |
Description | An experimental and computational methodology to fully quantify the kinetics of electrocatalytic reduction of O2 catalysed by multicopper oxidases. |
Type Of Material | Technology assay or reagent |
Year Produced | 2012 |
Provided To Others? | Yes |
Impact | Too early to say. |
URL | http://dx.doi.org/10.1039/C2SC00632D |
Title | Code associated with "A sensitivity metric and software to guide the analysis of soft films measured by a quartz crystal microbalance" |
Description | MATLAB code with a graphical user inter- face to enable other QCM users to employ this analysis. The current software can be applied to any single, homogeneous adlayer that obeys a Kelvin-Voigt viscoelastic model and sits under a semi-infinite Newtonian fluid. |
Type Of Technology | Software |
Year Produced | 2016 |
Open Source License? | Yes |
Impact | None to date |
Title | Matlab code for modelling electrocatalytic oxygen reduction in multicopper oxidases |
Description | A set of Matlab routines, linked to and described in the associated Chem. Sci. article, that allows one to convert enzyme responses to electrochemical stimuli and turn them into catalytic rate constants. |
Type Of Technology | Software |
Year Produced | 2012 |
Open Source License? | Yes |
Impact | Too soon to tell. |
URL | http://dx.doi.org/10.1039/C2SC00632D |