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Advances in enzyme bioelectrochemistry

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2018, Anais da Academia Brasileira de Ciencias

https://doi.org/10.1590/0001-3765201820170514
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Abstract

Bioelectrochemistry can be defined as a branch of Chemical Science concerned with electron-proton transfer and transport involving biomolecules, as well as electrode reactions of redox enzymes. The bioelectrochemical reactions and system have direct impact in biotechnological development, in medical devices designing, in the behavior of DNA-protein complexes, in green-energy and bioenergy concepts, and make it possible an understanding of metabolism of all living organisms (e.g. humans) where biomolecules are integral to health and proper functioning. In the last years, many researchers have dedicated itself to study different redox enzymes by using electrochemistry, aiming to understand their mechanisms and to develop promising bioanodes and biocathodes for biofuel cells as well as to develop biosensors and implantable bioelectronics devices. Inside this scope, this review try to introduce and contemplate some relevant topics for enzyme bioelectrochemistry, such as the immobilizati...

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Fully integrated biocatalytic electrodes based on bioaffinity interactions1This paper was a finalist for the Biosensors & Bioelectronics Award for the most original contribution to the Congress.1
Amos Bardea

Biosensors and Bioelectronics, 1998

Integrated bioelectrocatalytically active electrodes are assembled by the deposition of enzymes onto respective electrically contacted affinity matrices and further cross-linking of the enzyme monolayers. A catalyst-NAD +-dyad for the binding of the NAD +dependent enzymes and cytochrome-like molecules for the binding of the heme-protein-dependent enzymes are used to construct integrated electrically contacted biocatalytic systems. NAD +-dependent lactate dehydrogenase (LDH) is assembled onto a pyrroloquinoline quinone-NAD + monolayer. The redox-active monolayer is organized via covalent attachment of pyrroloquinoline quinone (PQQ) to a cystamine monolayer associated with a Au-electrode, followed by covalent linkage of N 6-(2-aminoethyl)-NAD + to the monolayer. The interface modified with the PQQ-NAD +-dyad provides temporary affinity binding for LDH and allows cross-linking of the enzyme monolayer. The cross-linked LDH is bioelectrocatalytically active towards oxidation of lactate. The bioelectrocatalyzed process involves the PQQ-mediated oxidation of the immobilized NADH. Integrated, electrically contacted bioelectrodes are produced by the affinity binding and further cross-linking of nitrate reductase (NR) (cytochrome-dependent, E.C. 1.9.6.1 from E. coli) or Co II-protoporphyrin IX reconstituted myoglobin (Co II-Mb) atop the microperoxidase-11 (MP-11) monolayer associated with a Au-electrode. The MP-11 monolayer provides an affinity interface for the temporary binding of the enzymes, that allows the cross-linkage of the enzyme molecules. The MP-11 assembly acts as electron transfer mediator for the reduction of the secondary enzyme layer. The integrated bioelectrodes consisting of NR and Co II-Mb show catalytic activities for NO 3 − reduction and acetylenedicarboxylic acid hydrogenation, respectively. Two Fe III-protoporphyrin IX units are reconstituted into a four ␣-helix bundle de novo protein assembled as a monolayer on a Au-electrode. Vectorial electron transfer proceeds in the synthetic heme-protein monolayer. Cross-linking of an affinity complex generated between the Fe III-protoporphyrin IX reconstituted de novo protein monolayer and NR yields an integrated, electrically contacted enzyme electrode that stimulates the bioelectrocatalyzed reduction of nitrate.

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    cristina cordas

    Electroanalysis

    Nitric oxide radical (NO) is a signalling molecule involved in virtually all forms of life. Its relevance has been leading to the development of different analytical methodologies to assess the temporal and spatial fluxes of NO under the complex biological milieu. Third-generation electrochemical biosensors are promising tools for in loco and in vivo NO quantification and, over the past years, heme proteins and porphyrins have been used in their design. Since there are some limitations with the biorecognition element directly adsorbed onto the electrode surface, nanomaterials (carbon nanotubes, gold nanoparticles, etc.) and polymers (cellulose, chitosan, nafion , polyacrylamide, among others) have been explored to achieve high kinetics and better biosensor performance. In this review, a broad overview of the field of electrochemical third-generation biosensors for NO electroanalysis is presented, discussing their main characteristics and aiming new outlooks and advances in this field.

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    Electrochemical Biosensors Containing Pure Enzymes or Crude Extracts as Enzyme Sources for Pesticides and Phenolic Compounds with Pharmacological Property Detection and Quantification
    Tatiana Martins

    IntechOpen eBooks, 2019

    Biosensors are chemical sensors in which the recognition system is based on a biochemical mechanism. They perform the specific component detection in a sample through an appropriate analytical signal. Enzyme-based biosensors are the most prominent biosensors because of their high specificity and selectivity; besides being an alternative to the common immunosensors, they are more expensive and present a limited binding capacity with the antigen depending on assay conditions. This chapter approaches the use of enzymes modified electrodes in amperometric biosensing application to detect and quantify pesticides and phenolic compounds with pharmacological properties, as they have been a promising analytical tool in environmental monitoring. These biosensors may be prepared from pure enzymes or their crude extracts. Pure enzyme-based biosensors present advantages as higher substrate specificity and selectivity when compared to crude extract enzymatic biosensors; nevertheless, the enzyme high costs are their drawbacks. Enzymatic crude extract biosensors show lower specificity due to the fact that they may contain more than one type of enzyme, but they may be obtained from low-cost fabrication methods. In addition, they can contain enzyme cofactors besides using the enzyme in its natural conformation.

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