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  • 1.
    Aleksejeva, Olga
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Sokolov, A. V.
    Russia Saint-Petersburg State University, Russia.
    Marquez, I.
    University of Seville, Spain.
    Gustafsson, Anna
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Bushnev, S.
    Russian Academy of Sciences, Russia.
    Eriksson, Håkan
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ljunggren, Lennart
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shleev, Sergey
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Russian Academy of Sciences, Russia.
    Autotolerant ceruloplasmin based biocathodes for implanted biological power sources2021In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 140Article in journal (Refereed)
    Abstract [en]

    High-performance autotolerant bioelectrodes should be ideally suited to design implantable bioelectronic devices. Because of its high redox potential and ability to reduce oxygen directly to water, human ceruloplasmin, HCp, the only blue multicopper oxidase present in human plasma, appears to be the ultimate biocatalyst for oxygen biosensors and also biocathodes in biological power sources. In comparison to fungal and plant blue multicopper oxidases, e.g. Myrothecium verrucaria bilirubin oxidase and Rhus vernicifera laccase, respectively, the inflammatory response to HCp in human blood is significantly reduced. Partial purification of HCp allowed to preserve the native conformation of the enzyme and its biocatalytic activity. Therefore, electrochemical studies were carried out with the partially purified enzyme immobilised on nanostructured graphite electrodes at physiological pH and temperature. Amperometric investigations revealed low reductive current densities, i.e. about 1.65 µA cm−2 in oxygenated electrolyte and in the absence of any mediator, demonstrating nevertheless direct electron transfer based O2 bioelectroreduction by HCp for the first time. The reductive current density obtained in the mediated system was about 12 µA cm−2. Even though the inflammatory response of HCp is diminished in human blood, inadequate bioelectrocatalytic performance hinders its use as a cathodic bioelement in a biofuel cell.

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  • 2.
    Andoralov, Victor
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shleev, Sergey
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.
    Dergousova, Natalia
    Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.
    Kulikova, Olga
    Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.
    Popov, Vladimir
    Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia; Kurchatov NBIC Centre, National Research Centre “Kurchatov Institute”, 123182 Moscow, Russia.
    Tikhonova, Tamara
    Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.
    Octaheme nitrite reductase: The mechanism of intramolecular electron transfer and kinetics of nitrite bioelectroreduction.2021In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 138, article id 107699Article in journal (Refereed)
    Abstract [en]

    Detailed impedance and voltammetric studies of hexameric octaheme nitrite reductase immobilized on carbon-based nanomaterials, specifically nanotubes and nanoparticles, were performed. Well-pronounced bioelectrocatalytic reduction of nitrite on enzyme-modified electrodes was obtained. Analysis of the impedance data indicated the absence of long-lived intermediates involved in the nitrite reduction. Cyclic voltammograms of biomodified electrodes had a bi-sigmoidal shape, which pointed to the presence of two enzyme orientations on carbon supports. The maximum (limiting) catalytic currents were determined and, by applying the correction by the mixed kinetics equation, the Tafel dependences were plotted for each catalytic wave/each enzyme orientation. Finally, two schemes for the rate-limiting processes during bioelectrocatalysis were proposed, viz. for low- and high-potential orientations.

  • 3. Di Bari, Chiara
    et al.
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    De Lacey, Antonio
    Pita, Marcos
    Laccase-​modified gold nanorods for electrocatalytic reduction of oxygen2016In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 107, p. 30-36Article in journal (Refereed)
    Abstract [en]

    The multicopper oxidase Trametes hirsuta laccase (ThLc) served as a bioelectrocatalyst on nanostructured cathodes. Nanostructuring was provided by gold nanorods (AuNRs)​, which were characterized and covalently attached to electrodes made of low-​d. graphite. The nanostructured electrode was the scaffold for covalent and oriented attachment of ThLc. The bioelectrocatalytic currents measured for oxygen redn. were as high as 0.5 mA​/cm2 and 0.7 mA​/cm2, which were recorded under direct and mediated electron transfer regimes, resp. The exptl. data were fitted to math. models showing that when the O2 is bioelectroreduced at high rotation speed of the electrode the heterogeneous electron transfer step is the rate-​liming stage. The electrochem. measurement hints a wider population of non-​optimally wired laccases than previously reported for 5-​8 nm size Au nanoparticle-​modified electrode, which could be due to a larger size of the AuNRs when compared to the laccases as well as their different crystal facets.

  • 4. Krikstolaityte, Vida
    et al.
    Barrantes, Alejandro
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ramanavicius, Arunas
    Arnebrant, Thomas
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ruzgas, Tautgirdas
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Bioelectrocatalytic reduction of oxygen at gold nanoparticles modified with laccase2014In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 95, p. 1-6Article in journal (Refereed)
    Abstract [en]

    To characterise bioelectrocatalytic oxygen reduction at gold nanoparticles (AuNPs) modified with Trametes hirsuta laccase (ThLc) combined electrochemical and quartz crystal microbalance measurements have been used. The electrodes with different degrees of AuNP-monolayer coverage, theta, have been studied. In every case of theta close to theoretically possible 44 ThLc molecules adsorbed at 22 nm diameter AuNP. The bioelectrocatalytic current was recalculated down to the current at a single AuNR Unexpectedly, the current at a single AuNP was higher when theta was higher. The maximum current reached at a single AuNP was 31.10(-18) A which corresponds to the enzyme turnover (k(cat)) 13 s(-1). This rate is lower than the homogeneous ThLc turnover (190 s(-1)) suggesting partial denaturation of ThLc upon adsorption or that some ThLc are not in DET contact with the electrode surface

  • 5.
    Lamberg, P.
    et al.
    Department of Chemistry, University of Rochester, 14611 Rochester, NY, USA.
    Hamit-Eminovski, J.
    CMC Diabetes Formulation Development, Novo Nordisk, Novo Alle Bagsvaerd, 2880, Denmark.
    Toscano, M. D.
    Protein Engineering, Novozymes A/S, Bagsvaerd 2880, Denmark.
    Eicher-Lorka, O.
    Department of Organic Chemistry, Center for Physical Sciences and Technology, Sauletekio av. 3, LT-10257 Vilnius, Lithuania.
    Niaura, G.
    Department of Organic Chemistry, Center for Physical Sciences and Technology, Sauletekio av. 3, LT-10257 Vilnius, Lithuania.
    Arnebrant, Thomas
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ruzgas, Tautgirdas
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Electrical activity of cellobiose dehydrogenase adsorbed on thiols: Influence of charge and hydrophobicity2017In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 115, p. 26-32Article in journal (Refereed)
    Abstract [en]

    The interface between protein and material surface is of great research interest in applications varying from implants, tissue engineering to bioelectronics. Maintaining functionality of bioelements depends greatly on the immobilization process. In the present study direct electron transfer of cellobiose dehydrogenase from Humicola insolens (HiCDH), adsorbed on four different self-assembled monolayers (SAMs) formed by 5-6 chain length carbon thiols varying in terminal group structure was investigated. By using a combination of quartz crystal micro balance with dissipation, ellipsometry and electrochemistry the formation and function of the HiCDH film was studied. It was found that the presence of charged pyridinium groups was needed to successfully establish direct electron contact between the enzyme and electrode. SAMs formed from hydrophilic charged thiols achieved nearly two times higher current densities compared to hydrophobic charged thiols. Additionally, the results also indicated proportionality between HiCDH catalytic constant and water content of the enzyme film. Enzyme films on charged pyridine thiols had smaller variations in water content and viscoelastic properties than films adsorbed on the more hydrophobic thiols. This work highlights several perspectives on the underlying factors affecting performance of immobilized HiCDH. (C) 2017 Elsevier B.V. All rights reserved.

  • 6. Pita, Marcos
    et al.
    Gutierrez-Sanchez, Cristina
    Toscano, Miguel
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    De Lacey, Antonio
    Oxygen biosensor based on bilirubin oxidase immobilized on a nanostructured gold electrode2013In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 94, p. 69-74Article in journal (Refereed)
    Abstract [en]

    Gold disk electrodes modified with gold nanoparticles have been used as a scaffold for the covalent immobilization of bilirubin oxidase. The nanostructured bioelectrodes were tested as mediator-​less biosensors for oxygen in a buffer that mimics the content and the compn. of human physiol. fluids. Chronoamperometry measurements showed a detection limit towards oxygen of 6 ± 1 μM with a linear range of 6-​300 μM, i.e. exceeding usual physiol. ranges of oxygen in human tissues and fluids. The biosensor presented is the first ever-​reported oxygen amperometric biosensor based on direct electron transfer of bilirubin oxidase.

  • 7.
    Psotta, Carolin
    et al.
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Aptusens AB, S-29394 Kyrkhult, Sweden..
    Cirovic, Stefan
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Gudmundsson, Petri
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Falk, Magnus
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Mandal, Tanushree
    Univ Galway, Sch Chem & Ryan Inst, Univ Rd, Galway, Ireland..
    Reichhart, Thomas
    Univ Nat Resources & Life Sci, Dept Food Sci & Technol, BOKU, A-1190 Vienna, Austria.;DirectSens Biosensors GmbH, A-3400 Klosterneuburg, Austria..
    Leech, Donal
    Univ Galway, Sch Chem & Ryan Inst, Univ Rd, Galway, Ireland..
    Ludwig, Roland
    Univ Nat Resources & Life Sci, Dept Food Sci & Technol, BOKU, A-1190 Vienna, Austria.;DirectSens Biosensors GmbH, A-3400 Klosterneuburg, Austria..
    Kittel, Roman
    Univ Nat Resources & Life Sci, Dept Food Sci & Technol, BOKU, A-1190 Vienna, Austria..
    Schuhmann, Wolfgang
    Ruhr Univ Bochum, Fac Chem & Biochem, Analyt Chem Ctr Electrochem Sci, D-44780 Bochum, Germany..
    Shleev, Sergey
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Aptusens AB, S-29394 Kyrkhult, Sweden..
    Continuous ex vivo glucose sensing in human physiological fluids using an enzymatic sensor in a vein replica2023In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 152, article id 108441Article in journal (Refereed)
    Abstract [en]

    Managing blood glucose can affect important clinical outcomes during the intraoperative phase of surgery. However, currently available instruments for glucose monitoring during surgery are few and not optimized for the specific application. Here we report an attempt to exploit an enzymatic sensor in a vein replica that could continuously monitor glucose level in an authentic human bloodstream. First, detailed investigations of the superficial venous systems of volunteers were carried out using ocular and palpating examinations, as well as advanced ultrasound measurements. Second, a tubular glucose-sensitive biosensor mimicking a venous system was designed and tested. Almost ideal linear dependence of current output on glucose concentration in phosphate buffer saline was obtained in the range 2.2-22.0 mM, whereas the dependence in human plasma was less linear. Finally, the developed biosensor was investigated in whole blood under homeostatic conditions. A specific correlation was found between the current output and glucose concentration at the initial stage of the biodevice operation. However, with time, blood coagulation during measurements negatively affected the performance of the biodevice. When the experimental results were remodeled to predict the response without the influence of blood coagulation, the sensor output closely followed the blood glucose level.

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  • 8.
    Rajendran, Sriram Thoppe
    et al.
    Technical University of Denmark.
    Huszno, Kinga
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Dębowski, Grzegorz
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces.
    Sotres, Javier
    Malmö University, Biofilms Research Center for Biointerfaces. Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Ruzgas, Tautgirdas
    Malmö University, Biofilms Research Center for Biointerfaces. Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Boisen, Anja
    Technical University of Denmark,.
    Zór, Kinga
    Technical University of Denmark,.
    Tissue-based biosensor for monitoring the antioxidant effect of orally administered drugs in the intestine2020In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 138, article id 107720Article in journal (Refereed)
    Abstract [en]

    For a better understanding of the effect of drugs and their interaction with cells and tissues, there is a need for in vitro and ex vivo model systems which enables studying these events. There are several in vitro methods available to evaluate the antioxidant activity; however, these methods do not factor in the complex in vivo physiology. Here we present an intestinal tissue modified oxygen electrode, used for the detection of the antioxidant effect of orally administered drugs in the presence of H2O2. Antioxidants are essential in the defense against oxidative stress, more specifically against reactive oxygen species such as H2O2. Due to the presence of native catalase in the intestine, with the tissue-based biosensor we were able to detect H2O2 in the range between 50 and 500 µM. The reproducibility of the sensor based on the calculated relative standard deviations was 15 ± 6%. We found that the O2 production by catalase from H2O2 was reduced in the presence of a well-known antioxidant, quinol. This indirectly detected antioxidant activity was also observed in the case of orally administered drugs with a reported anti-inflammatory effect such as mesalazine and paracetamol, while no antioxidant activity was recorded with aspirin and metformin.

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  • 9. Salaj-Kosla, Urszula
    et al.
    Poller, Sascha
    Schuhmann, Wolfgang
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Magner, Edmond
    Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes2013In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 91, p. 15-20Article in journal (Refereed)
    Abstract [en]

    The enzyme Trametes hirsuta laccase undergoes direct electron transfer at unmodified nanoporous gold electrodes, displaying a c.d. of 28 μA​/cm2. The response indicates that ThLc was immobilized at the surface of the nanopores in a manner which promoted direct electron transfer, in contrast to the absence of a response at unmodified polycryst. gold electrodes. The bioelectrocatalytic activity of ThLc modified nanoporous gold electrodes was strongly dependent on the presence of halide ions. Fluoride completely inhibited the enzymic response, whereas in the presence of 150 mM Cl-​, the current was reduced to 50​% of the response in the absence of Cl-​. The current increased by 40​% when the temp. was increased from 20 °C to 37 °C. The response is limited by enzymic and​/or enzyme electrode kinetics and is 30​% of that obsd. for ThLc co-​immobilized with an osmium redox polymer.

  • 10.
    Shleev, Sergey
    Malmö högskola, Faculty of Health and Society (HS).
    Direct electron transfer reactions between human ceruloplasmin and electrodes2009In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 76, no 1-2, p. 34-41Article in journal (Refereed)
    Abstract [en]

    In an effort to find conditions favoring bioelectrocatalytic redn. of oxygen by surface-immobilized human ceruloplasmin (Cp), direct electron transfer (DET) reactions between Cp and an extended range of surfaces were considered. Exploiting advances in surface nanotechnol., bare and carbon-nanotube-modified spectrog. graphite electrodes as well as bare, thiol- and gold-nanoparticle-modified gold electrodes were considered, and ellipsometry provided clues as to the amt. and form of adsorbed Cp. DET was studied under different conditions by cyclic voltammetry and chronoamperometry. Two Faradaic processes with midpoint potentials of about 400 mV and 700 mV vs. NHE, corresponding to the redox transformation of copper sites of Cp, were clearly obsd. In spite of the significant amt. of Cp adsorbed on the electrode surfaces, as well as the quite fast DET reactions between the redox enzyme and electrodes, bioelectrocatalytic redn. of oxygen by immobilized Cp was never registered. The bioelectrocatalytic inertness of this complex multi-functional redox enzyme interacting with a variety of surfaces might be assocd. with a very complex mechanism of intramol. electron transfer involving a kinetic trapping behavior.

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  • 11.
    Shleev, Sergey
    et al.
    Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö högskola, Biofilms Research Center for Biointerfaces.
    Bergel, Alain
    Gorton, Lo
    Biological fuel cells: Divergence of opinion2015In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 106, no Part A, p. 1-2Article in journal (Other academic)
    Abstract [en]

    Editorial

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  • 12.
    Shleev, Sergey
    et al.
    Malmö högskola, Faculty of Health and Society (HS).
    Jarosz-Wilkolazka, Anna
    Khalunina, Anna
    Morozova, Olga
    Yaropolov, Alexander
    Ruzgas, Tautgirdas
    Malmö högskola, Faculty of Health and Society (HS).
    Lo, Gorton
    Direct electron transfer reactions of laccases from different origins on carbon electrodes2005In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, no 67(1), p. 115-124Article in journal (Refereed)
  • 13. Stoica, Leonard
    et al.
    Ruzgas, Tautgirdas
    Malmö högskola, Faculty of Health and Society (HS).
    Gorton, Lo
    Electrochemical evidence of self-substrate inhibition as functions regulation for cellobiose dehydrogenase from Phanerochaete chrysosporium2009In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 76, no 1-2, p. 42-52Article in journal (Refereed)
    Abstract [en]

    The reaction mechanism of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium, adsorbed on graphite electrodes, was investigated by following its catalytic reaction with cellobiose registered in both direct and mediated electron transfer modes between the enzyme and the electrode. A wall-jet flow through amperometric cell housing the CDH-modified graphite electrode was connected to a single line flow injection system. In the present study, it is proven that cellobiose, at concentrations higher than 200 μM, competes for the reduced state of the FAD cofactor and it slows down the transfer of electrons to any 2e−/H+ acceptors or further to the heme cofactor, via the internal electron transfer pathway. Based on and proven by electrochemical results, a kinetic model of substrate inhibition is proposed and supported by the agreement between simulation of plots and experimental data. The implications of this kinetic model, called pseudo-ping-pong mechanism, on the possible functions CDH are also discussed. The enzyme exhibits catalytic activity also for lactose, but in contrast to cellobiose, this sugar does not inhibit the enzyme. This suggests that even if some other substrates are coincidentally oxidized by CDH, however, they do not trigger all the possible natural functions of the enzyme. In this respect, cellobiose is regarded as the natural substrate of CDH.

  • 14. Zebda, Abdelkader
    et al.
    Alcaraz, Jean-Pierre
    Vadgama, Pankaj
    Shleev, Sergey
    Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
    Minteer, Shelley D.
    Boucher, Francois
    Cinquin, Philippe
    Martin, Donald K.
    Challenges for successful implantation of biofuel cells2018In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 124, p. 57-72Article, review/survey (Refereed)
    Abstract [en]

    There is a growing interest in the design and engineering of operational biofuel cells that can be implanted. This review highlights the recent progress in the electrochemistry of biofuel cell technologies, but with a particular emphasis on the medical and physiological aspects that impact the biocompatibility of biofuel cells operating inside a living body. We discuss the challenge of supplying power to implantable medical devices, with regard to the limitations of lithium battery technology and why implantable biofuel cells can be a promising alternative to provide the levels of power required for medical devices. In addition to the challenge of designing a biofuel cell that provides a stable level of sufficient power, the review highlights the biocompatibility and biofouling problems of implanting a biofuel cell that have a major impact on the availability of the substrates inside body that provide fuel for the biofuel cell. These physiological challenges and associated ethical considerations are essential to consider for biofuel cells that are designed to be implanted for long-term operation inside a living animal and eventually to human clinical applications. (C) 2018 The Authors. Published by Elsevier B.V.

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