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  • The Electrochemical Society  (7)
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  • The Electrochemical Society  (7)
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  • 1
    Online-Ressource
    Online-Ressource
    The Electrochemical Society ; 2017
    In:  ECS Meeting Abstracts Vol. MA2017-01, No. 13 ( 2017-04-15), p. 867-867
    In: ECS Meeting Abstracts, The Electrochemical Society, Vol. MA2017-01, No. 13 ( 2017-04-15), p. 867-867
    Kurzfassung: Fast development of biomedical technology has led us to the invention and use of implantable medical devices to be utilized for direct monitoring of human health. In general, batteries is used as the main micropower supply of these implanted devices, however it has some drawbacks as it has to be replenished in due time. One of the promising continuous energy supplies to replace the use of batteries is enzyme biofuel cell (EBFC) which harvests electrical energy from the oxidation-reduction reactions as it generates electricity by glucose oxidation and oxygen reduction by the anode and cathode enzymes respectively; in which two of its main substrate are abundant and essential components in human physiological fluid. EBFC is expected to be minimal in size but still concerning to have maximized performance during operation including; high electrode potential range, current and power densities which dependent to the stability of the enzyme used and enzyme environment construction. In order to achieve long operation of EBFC, it is necessary to be assured that enzyme will not be denatured due to external potent factor such as shear stress, especially if EBFC is employed as micro-power supply of implanted devices in human in which the blood velocity will depend on the diameter of blood vessel as implantation site. One of the modest methods to protect immobilized enzyme from the shear stress is by using polymer such as Nafion to form physical entrapment layer. However, there is high possibility that Nafion as polymer will be degraded under shear stress leading to leaching of enzyme during long operation. Previous studies showed that encapsulated protein in porous materials, or immobilized inside layer by layer material showed more stability due to less exposure of the external stress. The use of mesoporous material such as sol-gels and entrapment in mesoporous silica have proven to increase the enzyme stability, however this materials are lack of conductivity which is not suitable for bioelectronics application. Due to the necessity of electrical communication, another study was employing conducting material such as Si wafer with micro culverts as enzyme protection platform which enhance the electron transfer between enzyme-electrodes material . The success of enzyme immobilization also depends on its carrier used for particular application. The platform for enzyme immobilization should have high capacity as enzyme anchoring sites, chemically stable, and having the structural ability to prolong enzyme stability. The combination of nanostructures with enzyme immobilization will be a promising direction since it is possible to engineer enzyme environment to limit the effect of external forces as called enzyme-in-cage. Carbon as the most popular and widely studied as electrode materials due to its physical and electrochemical stability properties as inert material, low cost and easy to be functionalized and decorated. Carbon can be used for miniaturized electrode fabricated through nanolithography by pyrolizing photoresist, decompose co-composite, leaving only carbon in microstructured pattern. The use of photoresist to form carbon after pyrolysis step has the advantage due to its ability to be patterned by photolithography techniques which is reproducible. The properties of pyrolized electrodes are comparable than glassy carbon electrode (GCE) which has similar electrochemical properties such as low background current as the effect of low capacitance Further advancement for this system is the integration of CNT which has high surface area, excellent conductivity due to its sp 2 carbon hybridization along its wall. In order to prevent any proximity effect of CNT-pyrolyzed carbon electrode, CNT was grown directly in carbon post in which the catalyst of CNT growth was deposited through electrostatic spray deposition (ESD). Grown CNT on pyrolyzed carbon is expected to keep high structural stability. In this study we elaborated the fabrication and application of CNT doped carbon microstructures (CNT-CME) as platform for enzyme confinement and immobilization. Thus eventually this method then applied to immobilize the FAD-dependent glucose dehydrogenase (FADGDH) α-subunit with menadione as mediator (FADGDH/menadione) system which has proven to have better performance as anode for biofuel cell application as its native character of low Km value. The parameter such as K m of free and immobilized enzyme, current and power densities of the EBFC were also tested. Figure 1
    Materialart: Online-Ressource
    ISSN: 2151-2043
    Sprache: Unbekannt
    Verlag: The Electrochemical Society
    Publikationsdatum: 2017
    ZDB Id: 2438749-6
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 2
    Online-Ressource
    Online-Ressource
    The Electrochemical Society ; 2017
    In:  ECS Meeting Abstracts Vol. MA2017-01, No. 44 ( 2017-04-15), p. 2034-2034
    In: ECS Meeting Abstracts, The Electrochemical Society, Vol. MA2017-01, No. 44 ( 2017-04-15), p. 2034-2034
    Kurzfassung: The field of enzyme based biofuel cells (EBFC) which utilize enzymes that can consume complex fuels (i.e. sucrose, fructose, etc.) and fuel mixtures to produce electrical energy has expanded over the last 3 decades, and it is now possible to consider applications for implantable fuel cells, bio-battery and aquatic device power source. The last three decades have seen major advancements in the field to enhance the open circuit potentials, current and power densities, fuel efficiency and biocatalyst stability. These advances have resulted in open circuit potentials increasing from 175 mV to almost 1 V and current densities increasing from μA/cm 2 to mA/cm 2 . These increases come from enhanced electrochemically assessable surface areas with nanomaterials, increasing the oxidation reaction activity of anodes with enzyme cascades, metabolons, and optimal cell design to minimize internal resistance. However, further researches into improving power density over 1~5 mW are still needed to supply the power for stable operation of target devices. In this situation, the stable power output is hampered by a low level of electron transfer rate since electron transfer is known as crucial factor that determines performance of EBFC systems. The low level of electron transfer rate is resulted from several reasons that are related to protein structure and enzyme-layer formation. In detail, the redox center where electron is generated is often buried inside the protein matrix and moreover, enzymes are randomly oriented or forms multi-layers of enzymes during loaded on electrode, all of which attribute to long distance of electron transfer and degrade the performance of enzymatic electrode as well. To alleviate these problems, many groups have studied to develop the methods to enhance the electron transfer in these circumstances. Especially, construction of nanostructured high surface electrodes has been spotlighted because it could facilitate the electron transfer and thus performance of enzymatic electrode. In this research, we attempted to fabricate the nanostructured bioanode, optimizing the electron transfer from enzymes to electrode by control of enzyme layer thickness on the electrode surface. Genetically expressed FAD-dependent glucose dehydrogenase is immobilized on Au electrode modified by metal assisted chemical etching (MaCE). Recently, the fabrication of silicon (Si) subwavelength structure (SWS) by means of metal-assisted chemical etching (MaCE) has received increasing attention for its several merits during the modification of electrode surface that low-cost, fast, and scalable. Through this methodology, we fabricated nanospikes in pyramidal structure on the electrode surface, in which the nanospikes exist periodically with a sub-wavelength pitch all over the electrode surface. The effect of nanofabrication in this study is that immobilized enzyme on electrode surface are facilitated to be evenly distributed on the electrode surface. The periodically inclined structure grants equal opportunity of enzyme loading for unit area of electrode surface. By achieving the uniform distribution of enzymes, the distance between enzyme redox center and electrode surface can be reduced by excluding enzyme multilayers. Here, we experimentally studied the effect of pyramidal structure on enzymatic behaviors. During the experiment, the silicon (Si) wafer was selected with high conductive type for eliminating the possible overpotential that could be occured from the support material. Ag nanoparticles were used to assist the etching process of Si substrate, providing catalytic sites. The fabrication utilizing various diameter of Ag nanoparticles and etching times were conducted for having electrode candidates with different periodicities and pitch sizes. The optimized structure was confirmed by testing with electrochemical method, cyclic voltammetry (CV), and the optical slope which includes periodicity and pitch size was determined. Based on this research, it was concluded that electrode morphology is parameter that determines the performance of EBFC. Therefore, electrode structure for EBFC should be constructed in consideration of bio-electrode compatibility, not just of high surface area. Figure 1
    Materialart: Online-Ressource
    ISSN: 2151-2043
    Sprache: Unbekannt
    Verlag: The Electrochemical Society
    Publikationsdatum: 2017
    ZDB Id: 2438749-6
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 3
    Online-Ressource
    Online-Ressource
    The Electrochemical Society ; 2023
    In:  ECS Meeting Abstracts Vol. MA2023-01, No. 42 ( 2023-08-28), p. 2367-2367
    In: ECS Meeting Abstracts, The Electrochemical Society, Vol. MA2023-01, No. 42 ( 2023-08-28), p. 2367-2367
    Kurzfassung: In nature, most enzymes form a multienzyme complex called “metabolon” in the cellular system. The natural metabolon has been evolved to increase the efficiency of multi-step biocatalysis involved in such conditions. Such principle of enzymatic cascade reaction could be applied to the system which mimics pertinent reaction in vitro. Especially, its pertaining to bioelectrocatalytic system is quite promising to enhance its performance in terms of electrical generation or biochemical production, depending on systematic applications. In the previous studies , it was abundantly reported that multi-enzymatic reaction has been utilized to generate higher electrical current via sequential enzymatic oxidation of substrates ( e.g. , methanol, glucose, etc. ) in bioelectrochemical systems, and to operate biochemical production system utilizing multi-enzymic conversion or reduction reactions. However, it is still challenging to implement multi-step enzymatic reaction in the electrode platforms due to unmanageable regulations of inter-enzyme distance or electrical connection between enzymatic cofactor and electrode, during multi-enzyme co-immobilization on electrode surface. Herein, we intentionally design and construct variants of chimeric enzyme in which two enzymes, invertase (INV) and glucose dehydrogenase (GDH), are conjugated with peptide linkers. We expected that INV hydrolyzes sucrose into fructose and glucose, then glucose is oxidized at the catalytic subunit of GDH, releasing electrons toward the electrode. It also employed solid binding peptides (SBPs) fused to GDH in chimeric enzyme for the electrical connection of GDH-SBP and electrode. In order to accomplish the desired reaction with chimeric enzyme, we have conducted the following tests; 1) The recombinant plasmid harboring the genetic sequence of two enzymes with an in-between linker was constructed. 2) By production of chimeric proteins, the chain reaction efficiency of fusion constructs was compared depending on the length of the linker. 3) The gold binding peptide (GBP) was fused to sites (N- and C-terminus, or other sites) of the catalytic subunit of GDH. And finally, 4) the electron transfer rates were monitored and compared depending on the GBP tethering sites. Throughout the whole study, we found the factors affecting the occurrence of multienzyme cascade-based bioelectrochemical reactions and how to control these factors to improve the reaction efficiency Figure 1
    Materialart: Online-Ressource
    ISSN: 2151-2043
    Sprache: Unbekannt
    Verlag: The Electrochemical Society
    Publikationsdatum: 2023
    ZDB Id: 2438749-6
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 4
    Online-Ressource
    Online-Ressource
    The Electrochemical Society ; 2023
    In:  ECS Meeting Abstracts Vol. MA2023-01, No. 42 ( 2023-08-28), p. 2357-2357
    In: ECS Meeting Abstracts, The Electrochemical Society, Vol. MA2023-01, No. 42 ( 2023-08-28), p. 2357-2357
    Kurzfassung: The multienzyme complex in biological systems are highly ordered so that intermediate molecules occurred during enzymatic sequential reaction are efficiently delivered to downstream enzymes without diffused to bulk phase. Recently, the cascadic multienzymes have been adopted to enzymatic electrocatalytic platform to be applied for enzyme-based bioelectronics such as enzyme fuel cell, biosensors, and electrosynthetic system. This cascadic enzyme-electrode, in which interfacial electron transfer (ET) occurs concurrently with inter-enzyme chain reaction, has been regarded promising for the advancement of enzyme-based bioelectronics performance. However, co-regulation of interfacial electrical connection and inter-enzyme chain reaction efficiency has been known to be highly challenging due to systematic complexity. In this context, the generalized enzyme immobilization tool is significantly needed to be developed to control inter-enzyme and enzyme-electrode interface concurrently. Herein, enzyme cascade-based direct bioelectrocatalytic system has been constructed by immobilizing enzymes using the solid binding peptide (SBP) linker that can control surface-orientation of enzymes on electrode. Here, invertase (INV) and FAD-dependent glucose dehydrogenase gamma-alpha complex (GDHγα) were utilized as upstream- and downstream enzyme so that the sucrose hydrolysis (at INV) and glucose oxidation (at GDHγα) is concomitantly occurred. Especially, the GDHγα that is direct electron transfer (DET)-capable oxidoreductase, has bi-function that are downstream catalysis and transport of produced electrons toward electrode that cause bioelectrocatalytic current signal. To immobilize enzymes and control relative orientation of coupling enzymes, the SBP linker was tethered various termini (C-, N-, or both termini) of INV when SBP fusion site of GDHγα was fixed to C-terminus of GDH α subunit to enable efficient interfacial DET, based on previous study. Therefore, the inter-enzyme relative orientation dependent chain reaction efficiency was evaluated with resulting DET-based electrocatalytic current. In the result, it was found that the interfacial DET at GDHγα-electrode could be affected by binding conformation of co-immobilized enzyme, fusion INV. Most importantly, the chain reaction efficiency between INV and GDHγα was revealed to be diverse depending on different relative orientation determined by SBP tethering sites in enzymes. The intermediate delivery route was changed by relative positioning of coupling active sites, affecting overall cascade reaction rate. Taking into account the factors related with interfacial DET and intermediate delivery, precise design of bienzymatic electrode is indeed necessary in order to introduce SBP-tethering technique to cascadic enzyme-derived direct electrocatalytic platform. Figure 1
    Materialart: Online-Ressource
    ISSN: 2151-2043
    Sprache: Unbekannt
    Verlag: The Electrochemical Society
    Publikationsdatum: 2023
    ZDB Id: 2438749-6
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 5
    Online-Ressource
    Online-Ressource
    The Electrochemical Society ; 2012
    In:  ECS Meeting Abstracts Vol. MA2012-02, No. 43 ( 2012-06-04), p. 3203-3203
    In: ECS Meeting Abstracts, The Electrochemical Society, Vol. MA2012-02, No. 43 ( 2012-06-04), p. 3203-3203
    Kurzfassung: Abstract not Available.
    Materialart: Online-Ressource
    ISSN: 2151-2043
    Sprache: Unbekannt
    Verlag: The Electrochemical Society
    Publikationsdatum: 2012
    ZDB Id: 2438749-6
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 6
    In: Journal of The Electrochemical Society, The Electrochemical Society, Vol. 166, No. 12 ( 2019), p. F746-F754
    Materialart: Online-Ressource
    ISSN: 0013-4651 , 1945-7111
    RVK:
    Sprache: Englisch
    Verlag: The Electrochemical Society
    Publikationsdatum: 2019
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 7
    Online-Ressource
    Online-Ressource
    The Electrochemical Society ; 2020
    In:  ECS Journal of Solid State Science and Technology Vol. 9, No. 1 ( 2020-01-01), p. 015021-
    In: ECS Journal of Solid State Science and Technology, The Electrochemical Society, Vol. 9, No. 1 ( 2020-01-01), p. 015021-
    Kurzfassung: To enhance the light output of blue InGaN-based light emitting diodes (LEDs), a buried stripe-type n -electrode, expanded stripe-type p -electrode, and reflective p -bonding pad were employed. Flip-chip (FC) LEDs with the expanded p -electrode gave forward voltages of 2.99–3.11 V at 100 mA and series resistances of 3.28–3.94 Ω. The expanded p -electrode FCLED fabricated with 375 nm-thick window and TiO 2 adhesion layers produced 22.7% higher light output at 21 A/cm 2 than conventional FCLEDs. The expanded p -electrode FCLEDs revealed better current spreading efficiency than the c-FCLED, indicating the importance of the use of an optimised window and TiO 2 adhesion layers.
    Materialart: Online-Ressource
    ISSN: 2162-8769 , 2162-8777
    Sprache: Unbekannt
    Verlag: The Electrochemical Society
    Publikationsdatum: 2020
    Standort Signatur Einschränkungen Verfügbarkeit
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