Sensitive enzymatic determination of neurotransmitters in artificial sweat.

Dopamine (DA) and epinephrine (EN) are two phenolic molecules that are used in the human body and secreted in the brain actuating as neurotransmitters. As both molecules are highly important in the brain and the central nervous system, monitoring of their concentrations would enable better understanding of their importance and role in different physiological conditions. Copper efflux oxidase from Escherichia coli was shown in the past to have the ability of oxidizing polyphenolic compounds.

Use of Protein Engineering to Elucidate Electron Transfer Pathways between Proteins and Electrodes.

Herein, we review protein engineering tools for electron transfer enhancement and investigation in bioelectrochemical systems. We present recent studies in the field while focusing on how electron transfer investigation and measurements were performed and discuss the use of protein engineering to interpret electron transfer mechanisms.

Site-specifically wired and oriented glucose dehydrogenase fused to a minimal cytochrome with high glucose sensing sensitivity.

Direct electron transfer based enzymatic biosensors are highly efficient systems where electrons are transferred directly from the enzyme's electroactive site to the electrode. One way of achieving it is by 'wiring' the enzyme to the electrode surface. The wiring of enzymes to electrode surfaces can be reached in many different ways but controlling its orientation towards the electrode surface is still a challenge.

DNA/RNA Electrochemical Biosensing Devices a Future Replacement of PCR Methods for a Fast Epidemic Containment.

Pandemics require a fast and immediate response to contain potential infectious carriers. In the recent 2020 Covid-19 worldwide pandemic, authorities all around the world have failed to identify potential carriers and contain it on time. Hence, a rapid and very sensitive testing method is required.

Context effects of genetic code expansion by stop codon suppression.

Genetic code expansion enables the incorporation of unnatural amino acids into proteins thereby augmenting their physical and chemical properties. This is achieved by the reassignment of codons from their original sense to incorporate unnatural amino acids. The most commonly used methodology is stop codon suppression, which has resulted in numerous successful studies and applications in recent years.

Highly Efficient Flavin-Adenine Dinucleotide Glucose Dehydrogenase Fused to a Minimal Cytochrome C Domain.

Flavin-adenine dinucleotide (FAD) dependent glucose dehydrogenase (GDH) is a thermostable, oxygen insensitive redox enzyme used in bioelectrochemical applications. The FAD cofactor of the enzyme is buried within the proteinaceous matrix of the enzyme, which makes it almost unreachable for a direct communication with an electrode. In this study, FAD dependent glucose dehydrogenase was fused to a natural minimal cytochrome domain in its c-terminus to achieve direct electron transfer.