11 research outputs found
Optimization of Enzymatic Logic Gates and Networks for Noise Reduction and Stability
Biochemical computing attempts to process information with biomolecules and
biological objects. In this work we review our results on analysis and
optimization of single biochemical logic gates based on enzymatic reactions,
and a network of three gates, for reduction of the "analog" noise buildup. For
a single gate, optimization is achieved by analyzing the enzymatic reactions
within a framework of kinetic equations. We demonstrate that using
co-substrates with much smaller affinities than the primary substrate, a
negligible increase in the noise output from the logic gate is obtained as
compared to the input noise. A network of enzymatic gates is analyzed by
varying selective inputs and fitting standardized few-parameters response
functions assumed for each gate. This allows probing of the individual gate
quality but primarily yields information on the relative contribution of the
gates to noise amplification. The derived information is then used to modify
experimental single gate and network systems to operate them in a regime of
reduced analog noise amplification.Comment: 7 pages in PD
Towards Biochemical Filter with Sigmoidal Response to pH Changes: Buffered Biocatalytic Signal Transduction
We realize a biochemical filtering process by introducing a buffer in a
biocatalytic signal-transduction logic system based on the function of an
enzyme, esterase. The input, ethyl butyrate, is converted into butyric acid-the
output signal, which in turn is measured by the drop in the pH value. The
developed approach offers a versatile "network element" for increasing the
complexity of biochemical information processing systems. Evaluation of an
optimal regime for quality filtering is accomplished in the framework of a
kinetic rate-equation model.Comment: PDF, 23 page
Realization and Properties of Biochemical-Computing Biocatalytic XOR Gate Based on Enzyme Inhibition by a Substrate
We consider a realization of the XOR logic gate in a process biocatalyzed by
an enzyme (here horseradish peroxidase: HRP), the function of which can be
inhibited by a substrate (hydrogen peroxide for HRP), when the latter is
inputted at large enough concentrations. A model is developed for describing
such systems in an approach suitable for evaluation of the analog noise
amplification properties of the gate. The obtained data are fitted for gate
quality evaluation within the developed model, and we discuss aspects of
devising XOR gates for functioning in "biocomputing" systems utilizing
biomolecules for information processing
Biochemical Filter with Sigmoidal Response: Increasing the Complexity of Biomolecular Logic
Artificial Muscle Reversibly Controlled by Enzyme Reactions
Chemically induced actuation of a polypyrrole (Ppy) artificial muscle was controlled by biocatalytic reactions, resulting in changes in the redox state of the polymer film mediated by soluble redox species. The biocatalytic process triggered by diaphorase in the presence of NADH resulting in the reduction of the Ppy film was reflected by the potential shift in the negative direction generated in the film. Conversely, the biocatalytic process driven by laccase in the presence of O<sub>2</sub> resulted in the oxidation of the Ppy film, thus yielding the positive potential shift. Both reactions produced opposite bending of the Ppy flexible strip, allowing reversible actuation controlled by the biocatalytic processes. The biocatalytic reactions governing the chemical actuator can be extended to multistep cascades processing various patterns of biochemical signals and mimicking logic networks. The present chemical actuator exemplifies the first mechanochemical device controlled by biochemical means with the possibility to scale up the complexity of the biochemical signal-processing system
Bioelectrocatalytic Oxidation of Alkanes in a JP‑8 Enzymatic Biofuel Cell
Alkanes
are attractive fuels for fuel cells due to their high energy
density, but their use has not transitioned to biofuel cells. This
paper discusses the development of a novel enzyme cascade utilizing
alkane monooxygenase (AMO) and alcohol oxidase (AOx) to perform mediated
bioelectrocatalytic oxidation of hexane and octane. This was then
applied for the bioelectrocatalysis of the jet fuel JP-8, which was
tested directly in an enzymatic biofuel cell to evaluate performance.
The enzymatic catalysts were shown to be sulfur tolerant and produced
power densities up to 3 mW/cm<sup>2</sup> from native JP-8 without
desulfurization as opposed to traditional metal catalysts, which require
fuel preprocessing
Layer-by-Layer Assembled Carbon Nanotube-Acetylcholinesterase/Biopolymer Renewable Interfaces: SPR and Electrochemical Characterization
Developing
simple, reliable, and cost-effective methods of renewing
an inhibited biocatalyst (e.g., enzymatic interfaces) on biosensors
is needed to advance multiuse, reusable sensor applications. We report
a method for the renewal of layer-by-layer (LbL) self-assembled inhibition-based
enzymatic interfaces in multiwalled carbon nanotube (MWCNT) armored
acetylcholinesterase (AChE) biosensors. The self-assembly process
of MWCNT dispersed enzymes/biopolymers was investigated using surface
plasmon resonance (SPR). The LbL fabrication consisted of alternating
cushion layers of positively charged CNT-polyethylenimine (CNT-PEI)
and negatively charged CNT-deoxyribonucleic acid (CNT-DNA) and a functional
interface consisting of alternating layers of CNT-PEI and negatively
charged CNT-acetylcholine esterase (CNT-AChE, pH 7.4). The observed
SPR response signal increased while assembling the different layers,
indicating the buildup of multiple layers on the Au surface. A partial
desorption of the top enzymatic layer in the LbL structure was observed
with a desorption strategy employing alkaline treatment. This indicates
that the strong interaction of CNT-biopolymer conjugates with the
Au surface was a result of both electrostatic interactions between
biopolymers and the surface binding energy from CNTs: the closer the
layers are to the Au surface, the stronger the interactions. In contrast,
a similar LbL assembly of soluble enzyme/polyelectrolytes resulted
in stronger desorption on the surface after the alkaline treatment;
this led to the investigation of AChE layer removal, permanently inhibited
after pesticide exposure on glassy carbon (GC) electrodes, while keeping
the cushion layers intact. The desorption strategy permitted the SPR
and electrochemical electrode surfaces to be regenerated multiple
times by the subsequent self-assembly of fresh PEI/AChE layers. Flow-mode
electrochemical amperometric analysis demonstrated good stability
toward the determination of acetylcholine with 97.1 ± 2.7% renewability.
Our simple, inexpensive approach shows the potential of renewable
LbL self-assembled functional interfaces for multiple uses in a wide
field of applications such as biosensing, various biotechnological
processes, and the food and health industries