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Special Issue "Biomolecular Engineering and Bioelectronics"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Recognition".

Deadline for manuscript submissions: closed (31 March 2017).

Special Issue Editors

Prof. Dr. Koji Sode
E-Mail Website
Guest Editor
Joint Department of Biomedical Engineering, University of North Carolina at Chapel Hill (UNC) and North Carolina State University, Chapel Hill, NC, USA
Interests: protein engineering; enzyme engineering; biosensors; biosensing; biomedical engineering; biomolecular engineering
Dr. Shelley D. Minteer
E-Mail Website
Guest Editor
Department of Chemistry, University of Utah, Salt Lake City, UT 84112, USA
Interests: biofuel cells; biosensors; bioelectrocatalysis; electroanalysis
Dr. Seiya Tsujimura
E-Mail Website
Guest Editor
Division of Materials Science, Faculty of Pure and Applied Sciences, University of Tsukuba, Japan
Interests: bioelectrochemistry; electrochemistry; redox enzyme; biofuel cell; biosensor; mediator; direct electron transfer; mediator; mediated electron transfer; oxidase; dehydrogenase; porous carbon; carbon gel; carbon cryogel; bioelectrocatalysis; electrocatalyst
Dr. Jeffrey La Belle
E-Mail Website
Guest Editor
School of Biological and Health Systems Engineering, Arizona State University, USA
Interests: biosensors; wearable technologies; point-of-care technologies; sensing systems for health and environmental purposes

Special Issue Information

Dear Colleagues,

This Special Issue, “Biomolecular Engineering and Bioelectronics”, will cover advanced research topics relating to biomolecular engineering, focusing their application to bioelectronics, such as biosensing technologies and bio-fuel cell development. The research topics cover bioelectronics-based molecular studies, and basic studies on biomolecules, based on novel electrochemical approaches are also welcome. Topics of interests include, but are not limited to, research and development of novel biomolecules for future biosensing applications, advanced materials to be utilized as the interface between biological materials and electronic devices, novel electron acceptors to be utilized for electrochemical investigation of redox biochemistries, novel platform technologies for bioelectronics, such as novel electrode configuration and/or materials, novel principles for electrochemical based biosensing, such as advanced electrochemical impedance spectroscopy, novel concepts and technologies for bioelectronics based bioenergy generation, and so on. Research from both academic and industrial aspects is welcome.

Prof. Dr. Koji Sode
Prof. Dr. Shelley D. Minteer
Dr. Seiya Tsujimura
Dr. Jeffrey La Belle
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

 

Keywords

  • Biomolecular engineering
  • Biosensors
  • Biofuel cells
  • Bioelectronics
  • Electrochemistry
  • Diagnostic
  • Biodevices

Published Papers (2 papers)

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Research

Open AccessArticle
Micro-Electromechanical Affinity Sensor for the Monitoring of Glucose in Bioprocess Media
Int. J. Mol. Sci. 2017, 18(6), 1235; https://doi.org/10.3390/ijms18061235 - 08 Jun 2017
Cited by 6 | Viewed by 2185
Abstract
An affinity-viscometry-based micro-sensor probe for continuous glucose monitoring was investigated with respect to its suitability for bioprocesses. The sensor operates with glucose and dextran competing as binding partner for concanavalin A, while the viscosity of the assay scales with glucose concentration. Changes in [...] Read more.
An affinity-viscometry-based micro-sensor probe for continuous glucose monitoring was investigated with respect to its suitability for bioprocesses. The sensor operates with glucose and dextran competing as binding partner for concanavalin A, while the viscosity of the assay scales with glucose concentration. Changes in viscosity are determined with a micro-electromechanical system (MEMS) in the measurement cavity of the sensor probe. The study aimed to elucidate the interactions between the assay and a typical phosphate buffered bacterial cultivation medium. It turned out that contact with the medium resulted in a significant long-lasting drift of the assay’s viscosity at zero glucose concentration. Adding glucose to the medium lowers the drift by a factor of eight. The cglc values measured off-line with the glucose sensor for monitoring of a bacterial cultivation were similar to the measurements with an enzymatic assay with a difference of less than ±0.15 g·L−1. We propose that lectin agglomeration, the electro-viscous effect, and constitutional changes of concanavalin A due to exchanges of the incorporated metal ions may account for the observed viscosity increase. The study has demonstrated the potential of the MEMS sensor to determine sensitive viscosity changes within very small sample volumes, which could be of interest for various biotechnological applications. Full article
(This article belongs to the Special Issue Biomolecular Engineering and Bioelectronics)
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Open AccessArticle
Bimolecular Rate Constants for FAD-Dependent Glucose Dehydrogenase from Aspergillus terreus and Organic Electron Acceptors
Int. J. Mol. Sci. 2017, 18(3), 604; https://doi.org/10.3390/ijms18030604 - 10 Mar 2017
Cited by 18 | Viewed by 2218
Abstract
The flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Aspergillus species require suitable redox mediators to transfer electrons from the enzyme to the electrode surface for the application of bioelectrical devices. Although several mediators for FAD-GDH are already in use, they are still far [...] Read more.
The flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Aspergillus species require suitable redox mediators to transfer electrons from the enzyme to the electrode surface for the application of bioelectrical devices. Although several mediators for FAD-GDH are already in use, they are still far from optimum in view of potential, kinetics, sustainability, and cost-effectiveness. Herein, we investigated the efficiency of various phenothiazines and quinones in the electrochemical oxidation of FAD-GDH from Aspergillus terreus. At pH 7.0, the logarithm of the bimolecular oxidation rate constants appeared to depend on the redox potentials of all the mediators tested. Notably, the rate constant of each molecule for FAD-GDH was approximately 2.5 orders of magnitude higher than that for glucose oxidase from Aspergillus sp. The results suggest that the electron transfer kinetics is mainly determined by the formal potential of the mediator, the driving force of electron transfer, and the electron transfer distance between the redox active site of the mediator and the FAD, affected by the steric or chemical interactions. Higher k2 values were found for ortho-quinones than for para-quinones in the reactions with FAD-GDH and glucose oxidase, which was likely due to less steric hindrance in the active site in the case of the ortho-quinones. Full article
(This article belongs to the Special Issue Biomolecular Engineering and Bioelectronics)
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