Geoantineutrino Spectrum, 3He/4He-ratio Distribution in the Earth's Interior and Slow Nuclear Burning on the Boundary of the Liquid and Solid Phases of the Earth's Core

The description problem of geoantineutrino spectrum and reactor antineutrino experimental spectrum in KamLAND, which takes place for antineutrino energy \~2.8 MeV, and also the experimental results of the interaction of uranium dioxide and carbide with iron-nickel and silicaalumina melts at high pressure (5-10 GP?) and temperature (1600-2200C) have motivated us to consider the possible consequences of the assumption made by V.Anisichkin and coauthors that there is an actinid shell on boundary of liquid and solid phases of the Earth's core. We have shown that the activation of a natural nuclear reactor operating as the solitary waves of nuclear burning in 238U- and/or 232Th-medium (in particular, the neutron- fission progressive wave of Feoktistov and/or Teller-Ishikawa-Wood) can be such a physical consequence. The simplified model of the kinetics of accumulation and burnup in U-Pu fuel cycle of Feoktistov is developed. The results of the numerical simulation of neutron-fission wave in two-phase UO2/Fe medium on a surface of the Earth's solid core are presented. The georeactor model of 3He origin and the 3He/4He-ratio distribution in the Earth's interior is offered. It is shown that the 3He/4He ratio distribution can be the natural quantitative criterion of georeactor thermal power. On the basis of O'Nions-Evensen-Hamilton geochemical model of mantle differentiation and the crust growth supplied by actinid shell on the boundary of liquid and solid phases of the Earth's core as a nuclear energy source (georeactor with power of 30 TW), the tentative estimation of geoantineutrino intensity and geoantineutrino spectrum on the Earth surface are given.Comment: 28 pages, 12 figures. Added text, formulas, figures and references. Corrected equations. Changed content of some section

Solar System Processes Underlying Planetary Formation, Geodynamics, and the Georeactor

Only three processes, operant during the formation of the Solar System, are responsible for the diversity of matter in the Solar System and are directly responsible for planetary internal-structures, including planetocentric nuclear fission reactors, and for dynamical processes, including and especially, geodynamics. These processes are: (i) Low-pressure, low-temperature condensation from solar matter in the remote reaches of the Solar System or in the interstellar medium; (ii) High-pressure, high-temperature condensation from solar matter associated with planetary-formation by raining out from the interiors of giant-gaseous protoplanets, and; (iii) Stripping of the primordial volatile components from the inner portion of the Solar System by super-intense solar wind associated with T-Tauri phase mass-ejections, presumably during the thermonuclear ignition of the Sun. As described herein, these processes lead logically, in a causally related manner, to a coherent vision of planetary formation with profound implications including, but not limited to, (a) Earth formation as a giant gaseous Jupiter-like planet with vast amounts of stored energy of protoplanetary compression in its rock-plus-alloy kernel; (b) Removal of approximately 300 Earth-masses of primordial gases from the Earth, which began Earth's decompression process, making available the stored energy of protoplanetary compression for driving geodynamic processes, which I have described by the new whole-Earth decompression dynamics and which is responsible for emplacing heat at the mantle-crust-interface at the base of the crust through the process I have described, called mantle decompression thermal-tsunami; and, (c)Uranium accumulations at the planetary centers capable of self-sustained nuclear fission chain reactions.Comment: Invited paper for the Special Issue of Earth, Moon and Planets entitled Neutrino Geophysics Added final corrections for publicatio

Utilisation of an operative difficulty grading scale for laparoscopic cholecystectomy

Background A reliable system for grading operative difficulty of laparoscopic cholecystectomy would standardise description of findings and reporting of outcomes. The aim of this study was to validate a difficulty grading system (Nassar scale), testing its applicability and consistency in two large prospective datasets. Methods Patient and disease-related variables and 30-day outcomes were identified in two prospective cholecystectomy databases: the multi-centre prospective cohort of 8820 patients from the recent CholeS Study and the single-surgeon series containing 4089 patients. Operative data and patient outcomes were correlated with Nassar operative difficultly scale, using Kendall’s tau for dichotomous variables, or Jonckheere–Terpstra tests for continuous variables. A ROC curve analysis was performed, to quantify the predictive accuracy of the scale for each outcome, with continuous outcomes dichotomised, prior to analysis. Results A higher operative difficulty grade was consistently associated with worse outcomes for the patients in both the reference and CholeS cohorts. The median length of stay increased from 0 to 4 days, and the 30-day complication rate from 7.6 to 24.4% as the difficulty grade increased from 1 to 4/5 (both p < 0.001). In the CholeS cohort, a higher difficulty grade was found to be most strongly associated with conversion to open and 30-day mortality (AUROC = 0.903, 0.822, respectively). On multivariable analysis, the Nassar operative difficultly scale was found to be a significant independent predictor of operative duration, conversion to open surgery, 30-day complications and 30-day reintervention (all p < 0.001). Conclusion We have shown that an operative difficulty scale can standardise the description of operative findings by multiple grades of surgeons to facilitate audit, training assessment and research. It provides a tool for reporting operative findings, disease severity and technical difficulty and can be utilised in future research to reliably compare outcomes according to case mix and intra-operative difficulty

Thermal Properties of Graphene, Carbon Nanotubes and Nanostructured Carbon Materials

Recent years witnessed a rapid growth of interest of scientific and engineering communities to thermal properties of materials. Carbon allotropes and derivatives occupy a unique place in terms of their ability to conduct heat. The room-temperature thermal conductivity of carbon materials span an extraordinary large range - of over five orders of magnitude - from the lowest in amorphous carbons to the highest in graphene and carbon nanotubes. I review thermal and thermoelectric properties of carbon materials focusing on recent results for graphene, carbon nanotubes and nanostructured carbon materials with different degrees of disorder. A special attention is given to the unusual size dependence of heat conduction in two-dimensional crystals and, specifically, in graphene. I also describe prospects of applications of graphene and carbon materials for thermal management of electronics.Comment: Review Paper; 37 manuscript pages; 4 figures and 2 boxe

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

The Neisseriaceae family of bacteria causes a range of diseases including meningitis, septicaemia, gonorrhoea and endocarditis, and extracts haem from haemoglobin as an important iron source within the iron-limited environment of its human host. Herein we report crystal structures of apo- and haemoglobin-bound HpuA, an essential component of this haem import system. The interface involves long loops on the bacterial receptor that present hydrophobic side chains for packing against the surface of haemoglobin. Interestingly, our structural and biochemical analyses of Kingella denitrificans and Neisseria gonorrhoeae HpuA mutants, although validating the interactions observed in the crystal structure, show how Neisseriaceae have the fascinating ability to diversify functional sequences and yet retain the haemoglobin binding function. Our results present the first description of HpuA’s role in direct binding of haemoglobin

A Putative P-Type ATPase Required for Virulence and Resistance to Haem Toxicity in Listeria monocytogenes

Regulation of iron homeostasis in many pathogens is principally mediated by the ferric uptake regulator, Fur. Since acquisition of iron from the host is essential for the intracellular pathogen Listeria monocytogenes, we predicted the existence of Fur-regulated systems that support infection. We examined the contribution of nine Fur-regulated loci to the pathogenicity of L. monocytogenes in a murine model of infection. While mutating the majority of the genes failed to affect virulence, three mutants exhibited a significantly compromised virulence potential. Most striking was the role of the membrane protein we designate FrvA (Fur regulated virulence factor A; encoded by frvA [lmo0641]), which is absolutely required for the systemic phase of infection in mice and also for virulence in an alternative infection model, the Wax Moth Galleria mellonella. Further analysis of the ΔfrvA mutant revealed poor growth in iron deficient media and inhibition of growth by micromolar concentrations of haem or haemoglobin, a phenotype which may contribute to the attenuated growth of this mutant during infection. Uptake studies indicated that the ΔfrvA mutant is unaffected in the uptake of ferric citrate but demonstrates a significant increase in uptake of haem and haemin. The data suggest a potential role for FrvA as a haem exporter that functions, at least in part, to protect the cell against the potential toxicity of free haem

IlsA, A Unique Surface Protein of Bacillus cereus Required for Iron Acquisition from Heme, Hemoglobin and Ferritin

The human opportunistic pathogen Bacillus cereus belongs to the B. cereus group that includes bacteria with a broad host spectrum. The ability of these bacteria to colonize diverse hosts is reliant on the presence of adaptation factors. Previously, an IVET strategy led to the identification of a novel B. cereus protein (IlsA, Iron-regulated leucine rich surface protein), which is specifically expressed in the insect host or under iron restrictive conditions in vitro. Here, we show that IlsA is localized on the surface of B. cereus and hence has the potential to interact with host proteins. We report that B. cereus uses hemoglobin, heme and ferritin, but not transferrin and lactoferrin. In addition, affinity tests revealed that IlsA interacts with both hemoglobin and ferritin. Furthermore, IlsA directly binds heme probably through the NEAT domain. Inactivation of ilsA drastically decreases the ability of B. cereus to grow in the presence of hemoglobin, heme and ferritin, indicating that IlsA is essential for iron acquisition from these iron sources. In addition, the ilsA mutant displays a reduction in growth and virulence in an insect model. Hence, our results indicate that IlsA is a key factor within a new iron acquisition system, playing an important role in the general virulence strategy adapted by B. cereus to colonize susceptible hosts

Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells

In this study, different flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenases (FADGDHs) were characterized electrochemically after “wiring” them with an osmium redox polymer [Os(4,4′-dimethyl-2,2′-bipyridine)2(PVI)10Cl]+ on graphite electrodes. One tested FADGDH was that recently discovered in Glomerella cingulata (GcGDH), another was the recombinant form expressed in Pichia pastoris (rGcGDH), and the third was a commercially available glycosylated enzyme from Aspergillus sp. (AspGDH). The performance of the Os-polymer “wired” GDHs on graphite electrodes was tested with glucose as the substrate. Optimal operational conditions and analytical characteristics like sensitivity, linear ranges and current density of the different FADGDHs were determined. The performance of all three types of FADGDHs was studied at physiological conditions (pH 7.4). The current densities measured at a 20 mM glucose concentration were 494 ± 17, 370 ± 24, and 389 ± 19 μA cm−2 for GcGDH, rGcGDH, and AspGDH, respectively. The sensitivities towards glucose were 2.16, 1.90, and 1.42 μA mM−1 for GcGDH, rGcGDH, and AspGDH, respectively. Additionally, deglycosylated rGcGDH (dgrGcGDH) was investigated to see whether the reduced glycosylation would have an effect, e.g., a higher current density, which was indeed found. GcGDH/Os-polymer modified electrodes were also used and investigated for their selectivity for a number of different sugars

Enzymatic Glucose Based Bio batteries: Bioenergy to Fuel Next Generation Devices

[EN] This article consists of a review of the main concepts and paradigms established in the field of biological fuel cells or biofuel cells. The aim is to provide an overview of the current panorama, basic concepts, and methodologies used in the field of enzymatic biofuel cells, as well as the applications of these bio-systems in flexible electronics and implantable or portable devices. Finally, the challenges needing to be addressed in the development of biofuel cells capable of supplying power to small size devices with applications in areas related to health and well-being or next-generation portable devices are analyzed. The aim of this study is to contribute to biofuel cell technology development; this is a multidisciplinary topic about which review articles related to different scientific areas, from Materials Science to technology applications, can be found. With this article, the authors intend to reach a wide readership in order to spread biofuel cell technology for different scientific profiles and boost new contributions and developments to overcome future challenges.Financial support from the Spanish Ministry of Science, Innovation and University, through the State Program for Talent and Employability Promotion 2013-2016 by means of Torres Quevedo research contract in the framework of Bio2 project (PTQ-14-07145) and from the Instituto Valenciano de Competitividad Empresarial-IVACE-GVA (BioSensCell project)Buaki-Sogo, M.; García-Carmona, L.; Gil Agustí, MT.; Zubizarreta Saenz De Zaitegui, L.; García Pellicer, M.; Quijano-Lopez, A. (2020). Enzymatic Glucose Based Bio batteries: Bioenergy to Fuel Next Generation Devices. Topics in Current Chemistry (Online). 378(6):1-28. https://doi.org/10.1007/s41061-020-00312-8S1283786Schlögl R (2015) The revolution continues: Energiewende 2.0. Angew Chem Int Ed 54:4436–4439Mitcheson PD, Yeatman EM, Rao GK, Holmes AS, Green TC (2008) Energy harvesting from human and machine motion for wireless electronic devices. Proc IEEE 96(9):1457–1486Wang ZL, Wu W (2012) Nanotechnology-enabled energy harvesting for self-powered micro-/nanosystems. Angew Chem Int Ed 51:11700-11721Lamy C, Lima A, LeRhun V, Delime F, Coutanceau C, Léger J-M (2002) Recent advances in the development of direct alcohol fuel cells (DAFC). J Power Sources 105:283Cheng X, Shi Z, Glass N, Zhang L, Zhang J, Song D, Liu Z-S, Wang H, Shen J (2007) A review of PEM hydrogen fuel cell contamination: impacts, mechanisms, and mitigation. J Power Sources 165:739Boudghere Stambouli A, Traversa E (2002) Solid oxide fuel cells (SOFC): a review of an environmentally clean and efficient source of energy. Renew Sustain Energy Rev 6:433–455Qiao Y, Li CM (2011) Nanostructured catalyst in fuel cells. J Mater Chem 21:4027–4036Edwards PP, Kuznetsov VL, David WIF, Brandon NP (2008) Hydrogen and fuel cells: towards sustainable energy future. Energy Policy 36:4356–4362Kirubakaran A, Jain S, Nema RK (2009) A review on fuel cell technologies and power electronic interface. Renew Sustain Energy 13:2430–2440Kerzenmacher S, Ducree J, Zengerle R, von Stetten F (2008) An abiotically catalyzed glucose fuel cell for powering medical implants: reconstructed manufacturing protocol and analysis of performance. J Power Sources 182:66–75Drake RF, Kusserow BK, Messinger S, Matsuda S (1970) A tissue implantable fuel cell power supply. Trans Am Soc Artif Intern Organs 16:199–205Giner J, Holleck G, Malachesky PA (1973) Eine implantierbare Brennstoffzelle zum Betrieb eines mechanischen Herzens. Phys Chem 77:782–783. https://doi.org/10.1002/bbpc.19730771009Cosnier S, LeGoff A, Holzinger M (2014) Towards glucose biofuel cells implanted in human body for powering artificial organs: review. Electrochem Commun 38:19–23Katz E (2015) Implantable biofuel cells operating in vivo—potential power sources for bioelectronic devices. Bioelectron Med 2:1–12Bullen RA, Arnot TC, Lakeman JB, Walsh FC (2006a) Biofuel cells and their development . Biosens Bioelectron 21:2015–2045Cooney MJ, Svoboda V, Lau C, Martin G, Minteer SD (2008) Enzyme catalysed biofuel cells. Energy Environ Sci 1:320–337Cracknell JA, Vincent KA, Armstrong FA (2008) Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis. Chem Rev 108:2439–2461Sheldon RA (2007) Enzyme immobilization: the quest for optimum performance. Adv Synth Catal 349:1289–1307Bullen RA, Arnot TC, Lakeman JB, Walsh FC (2006b) Biofuel cells and their development. Biosens Bioelectron 21:2015–2045Koch C, Popiel D, Harnisch F (2014) Functional redundancy of microbial anodes fed by domestic wastewater. ChemElectroChem 1:1923–1931Mano N, Mao F, Heller A (2003) Characteristics of a miniature compartment-less glucose−O2 biofuel cell and its operation in a living plant. J Am Chem Soc 125(21):6588–6594Mano N, Mao F, Heller A (2002) A miniature biofuel cell operating in a physiological buffer. J Am Chem Soc 124(44):12962–12963Bruen D, Delaney C, Florea L, Diamond D (2017) Glucose sensing for diabetes monitoring: recent developments. Sensors 17:1866Falk M, Blum Z, Shleev S (2012) Direct electron transfer based enzymatic fuel cells. Electrochim Acta 82:191–202White HB (1976) Coenzymes as fossils of an earlier metabolic state. J Mol Evol 7:101–104Broderick JB (2001) Coenzymes and cofactors. In: eLS. Wiley, Chichester. https://www.els.net. https://doi.org/10.1038/npg.els.0000631Sakurai T, Kataoka K (2007) Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase. Chem Rec 7:220–229Bankar SB, Bule MV, Singhal RS, Ananthanarayan L (2009) Glucose oxidase—an overview. Biotech Adv 27:489–501Ferri S, Kojima K, Sode K (2011) Review of glucose oxidases and glucose dehydrogenases: a bird’s eye view of glucose sensing enzymes. J Diabetes Sci Technol 5:1068–1076Katz E, MacVittie K (2013) Implanted biofuel cells operating in vivo—methods, applications and perspectives—feature article. Energy Environ Sci 6:2791–2803Ghindilis AL, Atanasov P, Wilkins E (1997) Enzyme catalysed direct electron transfer: fundamentals and analytical applications. Electroanalysis 9:661–674Von Woedtke Th, Fisher U, Abel P (1994) Glucose oxidase electrodes: effect of H2O2 on enzyme activity? Biosens Bioelectron 9:65–71Kleppe K (1966) The effect of H2O2 on glucose oxidase from Aspergillus niger. Biochemistry 5:139–143Zebda A, Godran C, Le Goff A, Holzinger M, Cinquin P, Cosnier S (2011) Mediatorless high-power glucose biofuel cells based on compressed carbon nanotube-enzyme electrodes. Nat Commun 2:370Borenstein A, Hanna O, Attias R, Luski S, Brousse T, Aurbach D (2017) Carbon-based composite materials for supercapacitor electrodes: a review. J Mater Chem A 5:12653–12672Angione MD, Pilolli R, Cotrone S, Magliulo M, Mallardi A, Palazzo G, Sabbatini L, Fine D, Dodabalapur A, Lioffi N, Torsi L (2011) Carbon based nanomaterials for electronic bio-sensing. Mat Today 14:424–433Cha C, Shin SR, Annabi N, Dokmeci MR, Khademhosseini A (2013) Carbon based nanomaterials: multifunctional materials for biomedical engineering. ACS Nano 7:2891–2897Wang Z, Dai Z (2015) Carbon nanomaterials-based electrochemical biosensors: an overview. Nanoscale 7:6420–6431Jariwala D, Sangwan VK, Lauhon LJ, Marks TJ, Hersam MC (2013) Carbon nanomaterials for electronics, optoelectronics, photovoltaics and sensing. Chem Soc Rev 42:2824–2860Babadi AA, Bagheri S, Abdul Hamid SB (2016) Progress on implantable biofuel cell: nano-carbon functionalization for enzyme immobilization enhancement. Biosens Bioelectron 15:850–860Osadebe I, Leech D (2014) Effect of multi-walled carbon nanotubes on glucose oxidation by glucose oxidase or a flavin-dependent glucose dehydrogenase in redox-polymer-mediated enzymatic fuel cell anodes. ChemElectroChem 1:1988–1993Si P, Huang Y, Wang T, Ma J (2013) Nanomaterials for electrochemical non-enzymatic glucose biosensors. RSC Adv 3:3487–3502Putzbach W, Ronkainen NJ (2013) Immobilization techniques in the fabrication of nanomaterial-based electrochemical biosensors: a review. Sensors 13(4):4811–4840Walcarius A, Minteer SD, Wang J, Lin Y, Merkoçi A (2013) Nanomaterials for bio-functionalized electrodes: recent trends. J Mater Chem B 1:4878–4908Datta S, Christena LR, Rajaram YRS (2013) Enzyme immobilization: an overview on techniques and support materials. 3 Biotech 3(1):1–9Ivanov I, Vidaković-Koch T, Sundmaker K (2010) Recent advances in enzymatic fuel cells; experiments and modelling. Energies 3:803–846Nguyen HH, Kim M (2017) An overview of techniques in enzyme immobilization. Appl Sci Converg Technol 26(6):157–163Fu J, Reinhold J, Woodbury NW (2011) Peptide-modified surfaces for enzyme immobilization. PLoS One 6(4):e18692Lee DH, Park CH, Yeo JM, Kim SW (2006) Lipase immobilization on silica gel using a cross-linking method. J Ind Eng Chem 12(5):777–782Szymańska K, Bryjak J, Jarzębski AB (2009) Immobilization of invertase on mesoporous silicas to obtain hyper active biocatalysts. Top Catal 52:1030–1036Al-Lolage F, Meneghello M, Ma S, Ludwig R, Barlett PN (2017) A flexible method for the stable, covalent immobilization of enzymes at electrode surfaces. ChemElectroChem 4:1528–1534Gutierrez-Sanchez C, Shleev S, De Lacey AL, Pita M (2015) Third-generation oxygen amperometric biosensor based on Trametes hirsuta laccase covalently bound to graphite electrode. Chem Pap 69:237–240Pita M, Gutierrez-Sanchez C, Toscano MD, Shleev S, De Lacey AL (2013) Oxygen biosensor based on bilirubin oxidase immobilized on a nanostructured gold electrode. Bioelectrochemistry 94:69–74Vaz-Dominguez C, Campuzano S, Rüdiger O, Pita M, Gorbacheva M, Shleev S, Fernandez VM, de Lacey LA (2008) Laccase electrode for direct electrocatalytic reduction of O2 to H2O with high-operational stability and resistance to chloride inhibition. Biosens Bioelectron 24(4):531–537Gutiérrez-Sánchez C, Jia W, Beyl Y, Pita M, Schuhmann W, de Lacey LA, Stoica L (2012) Enhanced direct electron transfer between laccase and hierarchical carbon microfibers/carbon nanotubes composite electrodes. Comparison of three enzyme immobilization methods. Electrochim Acta 82:218–223Lv Y, Jin S, Wang Y, Lun Z, Xia C (2016) Recent advances in the application of nanomaterials in enzymatic glucose sensors. J Iran Chem Soc 13(10):1767–1776Zhao C, Gai P, Song R, Chen Y, Zhang J, Zhu J-J (2017) Nanostructured material-based biofuel cells: recent advances and future prospects. Chem Soc Rev 46:1545–1564Yu EH, Scott K (2010) Enzymatic biofuel cells—fabrication of enzyme electrodes. Energies 3:23–42Minteer SD, Atanassov P, Luckarift HR, Johnson GR (2013) New materials for biological fuel cells. Mater Today 15(4):166–173Sarma AK, Vatsyayan P, Goswami P, Minteer SD (2009) Recent advances in material science for developing enzyme electrodes. Biosens Bioelectron 24:2313–2322Jesionowski T, Zdarta J, Krajewska B (2014) Enzyme immobilization by adsorption: a review. Adsorption 20:801–821Sardar M, Gupta MN (2005) Immobilization of tomato pectinase on Con A-Seralose 4B by bioaffinity layering. Enzyme Microbial Technol 37:355–359Sheldon RA (2011) Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Appl Microbiol Biotechnol 92:467–477Velasco-Lozano S, López-Gallego F, Mateos-Díaz JC, Favela-Torres E (2015) Cross-linked enzyme aggregates (CLEA) in enzyme improvement—a review. Biocatalysis 1:166–177Cosnier S (1999) Biomolecule immobilization on electrode surfaces by entrapment or attachment to electrochemically polymerized films. A review. Biosen Bioelectron 14:443–456Heller A (1990) Electrical wiring of redox enzymes. Acc Chem Res 29:128–134Heller A (1992) Electrical connection of enzyme redox centres to electrodes. J Phys Chem 96:3579–3587Martins MVA, Pereira AR, Luz RAS, Iost RM, Crespilho FN (2014) Evidence of short-range electron transfer of a redox enzyme on graphene oxide electrodes. Phys Chem Chem Phys 16:17426–17436Luz RAS, Pereira AR, de Souza JCP, Sales FCPF, Crespilho FN (2014) Enzyme biofuel cells: thermodynamics. Kinetics and challenges in applicability. ChemElectroChem 1(11):1751–1777Neto SA, De Andrade AR (2013) New energy sources: the enzymatic biofuel cell. J Braz Chem Soc 24(12):1891–1912Rapoport BI, Kedzierski JT, Sarpeshkar R (2012) A glucose fuel cell for implantable brain–machine interfaces. PLoS One 7(6):6 e38436Zebda A, Alcaraz J-P, Vadgama P, Shleev S, Minteer SD, Boucher F, Cinquin P, Martin DK (2018) Challenges for successful implantation of biofuel cells. Bioelectrochemistry 124:57–72Ferraris RP, Diamond J (1997) Regulation of intestinal sugar transport. Physiol Rev 77:257–301Sprague JE, Arbeláez AM (2011) Glucose counterregulatory responses to hypoglicemia. Pediatr Endocrinol Rev 9:463–475Slaughter G, Kulkarni T (2019) Detection of human plasma glucose using a self-powered glucose biosensor. Energies 12:825Rathee K, Dhull V, Dhull R, Singh S (2016) Biosensors based on electrochemical lactate detection: a comprehensive review. Biochem Biophys Rep 5:35–54Koushanpour A, Gamella M, Katz E (2017) A biofuel cell based on biocatalytic reactions of lactate on both anode and cathode electrodes—extracting electrical power from human sweat. Electroanalysis 29:1602–1611Yao Y, Li H, Wang D, Liu C, Zhang C (2017) An electrochemiluminescence cloth-based biosensor with smartphone-based imaging for detection of lactate in saliva. Analyst 142:3715–3724Pankratov D, González-Arribas E, Blum Z, Shleev S (2016) Tear based bioelectronics. Electroanalysis 28:1250–1266Krogstad AL, Jansson PA, Gisslen P, Lönnroth P (1996) Microdialysis methodology for the measurement of dermal interstitial fluid in humans. Br J Dermatol 134(6):1005–1012Bandodkar AJ, Wang J (2016) Wearable biofuel cells: a review. Electroanalysis 28:1188–1200Jia W, Valdés-Ramírez G, Bandodkar AJ, Windmiller JR, Wang J (2013) Epidermal biofuel cells: energy harvesting from human perspiration. Angew Chem Int Ed 52:1–5Jeerapan I, Sempionatto JR, Pavinatto A, You J-M, Wang J (2016) Stretchable biofuel cells as wearable textile-based self-powered sensors. J Mater Chem A 4:18342–18353Valdés-Ramírez G, Li Y-G, Kima J, Jia W, Bandodkar AJ, Nuñez-Flores R, Miller PR, Wu S-Y, Narayan R, Windmiller JR, Polsky R, Wang J (2016) Microneedle-based self-powered glucose sensor. Electrochem Commun 47:58–62Gamella M, Koushanpour A, Katz E (2018) Biofuel cells—activation of micro- and macro- electronic devices. Bioelectrochemistry 119:33–42Mano N, Mao F, Shin W, Chen T, Heller A (2003) A miniature biofuel cell operating at 0.78 V. Chem Commun 20:518–519Shi B, Li Z, Fan Y (2018) Implantable energy harvesting devices. Adv Mater 30:1801511MacVittie K, Halámek J, Halámková L, Southcott M, Jemison WD, Lobel R, Katz E (2013) From “cyborg” lobsters to a pacemaker powered by implantable biofuel cells. Energy Environ Sci 6:81–86Szczupak A, Halámek J, Halámková L, Bocharova V, Alfonta L, Katz E (2012) Living battery—biofuel cells operating in vivo in clams. Energy Environ Sci 5:8891–8895Southcott M, MacVittie K, Halámek J, Halámková L, Jemison WD, Lobel R, Katz E (2013) A pacemaker powered by an implantable biofuel cell operating under conditions mimicking the human blood circulatory system—battery not included. Phys Chem Chem Phys 15:6278–6283MacVittie K, Conlon T, Katz E (2015) A wireless transmission system powered by an enzyme biofuel cell implanted in an orange. Bioelectrochemistry 106:28–33Aghahosseini H, Ramazani A, Asiabi PA, Gouranlou F, Hosseini F, Rezaei A, Min B-K, Joo SW (2016) Glucose-based biofuel cells: nanotechnology as a vital science in biofuel cell performance. Nanochem Res 1(2):83–204Zebda A, Cosnier S, Alcaraz J-P, Holzinger M, Le Goff A, Gondran C, Boucher F, Giroud F, Gorgy K, Lamraoui H, Cinquin P (2013) Single glucose biofuel cells implanted in rats power electronic devices. Sci Rep 2013:1516Ichi-Ribault SE, Alcaraz J-P, Boucher F, Boutaud B, Dalmolin R, Boutonnat J, Cinquin P, Zebda A, Martin DK (2018) Remote wireless control of an enzymatic biofuel cell implanted in a rabbit for 2 months. Electrochim Acta 269:360–366Bandodkar A (2017) Review—wearable biofuel cells: past, present and future. J Electrochem Soc 164(3):H3007–H3014Coman V, Ludwig R, Harreither W, Haltrich D, Gorton L, Ruzgas T, Shleev S (2010) A direct electron transfer-based glucose/oxygen biofuel cell operating in human serum. Fuel Cells 10(1):9–16Shoji K, Akiyama Y, Suzuki M, Nakamura N, Ohno H, Morishima K (2016) Biofuel cell backpacked insect and its application to wireless sensing. Biosens Bioelectron 78:390–395Reuillard B, Abreu C, Lalaoui N, Le Goff A, Holzinger M, Ondel O, Buret F, Cosnier S (2015) One-year stability for a glucose/oxygen biofuel cell combined with pH reactivation of the laccase/carbon nanotube biocathode. Bioelectrochemistry 106:73–76Sales FCPF, Iost RM, Martins MVA, Almeida MC, Crespilho FN (2013) An intravenous implantable glucose/dioxygen biofuel cell with modified flexible carbon fiber electrodes. Lab Chip 13:468Falk M, Narvez Villarrubia CW, Babanova S, Atanassov P, Shleev S (2013) Biofuel cells for biomedical applications: colonizing the animal kingdom. ChemPhysChem 14:2045–2058Rasmussen M, Ritzmann RE, Lee I, Pollack AJ, Scherson D (2012) An implantable biofuel cell for a live insect. J Am Chem Soc 134(3):1458–1460Halámková L, Halámek J, Bocharova V, Szczupak A, Alfonta L, Katz E (2012) Implanted biofuel cell operating in a living snail. J Am Chem Soc 134:5040–5043Cinquin P, Gondran C, Giroud F, Mazabrard S, Pellisier A, Boucher F, Alcaraz J-P, Gorgy K, Lenouvel F, Mathé S, Porcu P, Cosnier S (2010) A glucose biofuel cell implanted in rats. Plos One 5(5):e010476Chen C, Xie Q, Yang D, Xiao H, Fu Y, Tan S, Yao S (2013) Recent advances in electrochemical glucose biosensors: a review. RSC Adv 3:4473–4491Andoralov V, Falk M, Suyatin DB, Granmo M, Sotres J, Ludwig R, Popov VO, Schouenborg J, Blum Z, Shleev S (2013) Biofuel cell based on microscale nanostructured electrodes with inductive coupling to rat brain neuronsVerbeek MM, Leen WG, Willemsen MA, Slats D, Claassen JA (2016) Hourly analysis of cerebrospinal fluid glucose shows large diurnal fluctuations. J Cereb Blood F Met 36(5):899–902González-Guerrero MJ, Del Campo FJ, Esquivel JP, Leech D, Sabaté N (2017) Paper-based microfluidic biofuel cell operating under glucose concentrations within physiological range. Biosens Bioelectron 90:475–480Takeuchi ES, Leising RA (2002) Lithium batteries for biomedical applications. MRS Bull 27(8):624–627Bock DC, Marschilok A, Takeuchi KJ, Takeuchi ES (2012) Batteries used to power implantable biomedical devices. Electrochim Acta 84:155–164Greatbatch W, Lee JH, Mathias W, Eldridge M, Moser JR, Schneider AA (1971) The solid-state lithium battery: a new improved chemical power source for implantable cardiac pacemaker. IEEE Trans Biomed Eng 18(5):317–324Liu Y, Dong S (2007) A biofuel cell with enhanced power output by grape juice. Electrochem Commun 9(7):1423–1427Choi S, Lee H, Ghaffari R, Hyeon T, Kim D-H (2016) Recent advances in flexible and stretchable bio-electronic devices integrated with nanomaterials. Adv Mater 28:4203–4218Zhou L, Mao J, Ren Y, Han ST, Roy VAL, Zhou Y (2018) Recent advances of flexible data storage devices based on organic nanoscale materials. Small 14(10):1703126Gwon H, Kim H-S, Lee KU, Seo D-H, Park YC, Lee Y-S, Ahn BT, Kong K (2011) Flexible energy storage devices based on graphene paper. Energy Environ Sci 4:1277–1283Pang C, Lee C, Suh K-Y (2013) Recent advances in flexible sensors for wearable and implantable devices. J Appl Pol Sci 130:1429–1441Bandodkar AJ, Wang J (2014) Non-invasive wearable electrochemical sensors: a review. Trends Biotech 32(7):363–371Bandodkar AJ, Uia W, Wang J (2015) Tatto-based wearable electrochemical devices: a review. Electroanalysis 27(3):562–572Reid RC, Minteer SD, Gale BK (2015) Contact lens biofuel cell tested in a synthetic tear solution. Biosens Bioelectron 68:142Falk M, Andoralov V, Blum Z, Sotres J, Suyatin DM, Ruzgas T, Arnebrant T, Shleev S (2012) Biofuel cells as a power source for electronic contact lenses. Biosens Bioelectron 37(1):38–45Falk M, Andoralov V, Silow M, Toscano MD, Shleev S (2013) Miniature biofuel cell as a potential power source for Glucose-sensing contact lenses. Anal Chem 85(13):6342–6348Reid R, Jones SR, Hickey DP, Minteer SD, Gale BK (2016) Modeling carbon nanotubes connectivity and surface activity in a contact lens biofuel cell. Electrochim Acta 203:30–40Blum Z, Pankratov D, Shleev S (2014) Powering electronic contact lenses: current achievements, challenges and perspective. Expert Rev Ophthalmol 9(4):269–273Xiao X, Siepenkoetter T, Conghaile PÓ, Leech D, Magner E (2018) Nanoporous gold-based biofuel cell on contact lenses. ACS Appl Mater Interfaces 10(8):7107–7116Yang X-Y, Tian G, Jiang N, Su B-L (2012) Immobilization technology: a sustainable solution for biofuel cell design. Ener Environ Sci 5:5540–5563Mano N (2019) Engineering glucose oxidase for bioelectrochemical applications. Bioelectrochemistry 128:218–240Mate DM, Gonzalez-Perez D, Falk M, Kittl R, Pita M, De Lacey LA, Ludwig R, Shleev S, Alcalde M (2013) Blood tolerant caccase by directed evolution. Chem Biol 20:223–231Zhang L, Carucci C, Reculusa S, Goudeau B, Lefrançois P, Gounel S, Mano N, Kuhn A (2019) Rational design of enzyme-modified electrodes for optimized bioelectrocatalytic activity. ChemElectroChem 6(19):4980–4984Arechederra MN, Addo PK, Minteer SD (2011) Poly(neutral red) as a NAD+ reduction catalyst and a NADH oxidation catalyst: towards the development of a rechargeable biobattery. Electrochim Acta 56:1585Yang Y, Wang ZL (2015) Hybrid energy cells for simultaneously harvesting multi-types of energies. NanoEnergy 14:245–256Hansen BJ, Liu Y, Yang R, Wang ZL (2010) Hybrid nanogenerator for concurrently harvesting biomechanical and biochemical energy. ACS Nano 4:3647Song K, Han JH,