ПЕРСПЕКТИВЫ ИСПОЛЬЗОВАНИЯ ЛАККАЗ ДЛЯ РАЗРАБОТКИ БИОКАТОДОВ

1. Meredith M.T., Minteer, S.D. Biofuel cells: enhanced enzymatic bioelectrocatalysis. // Annu. Rev. Anal. Chem. 2012. V. 5. P. 157-179. doi:10.1146/annurev-anchem062011-143049;

2. Yoshida Н. Chemistry of lacquer (Urushi). Part I. Communication from the chemical society of Tokio // J. Chem. Soc. Trans. 1883. V. 43. P. 472-486;

3. Laccases. Anonymous Advances in Agricultural and Food Biotechnology. / Loera O., Pérez Pérez M., Irma Cristina. [et al]. // Research Signpost. 2006. P. 323-40;

4. Madhavi V., Lele S.S. Laccase: properties and applications. // BioResour 2009. V. 4. P. 1694-717;

5. Baldrian P. Fungal Laccases - Occurrence and Properties //FEMS Microbiology Reviews. 2006. V. 30. P. 215-242.

6. Thurston C.F. The Structure and Function of Fungal Laccases // Microbiolodgy. 1994. V. 140. P. 19-26;

7. Claus H. Laccases: structure, reactions, distribution // Micron. 2004. V. 35. P. 93-96;

8. "Голубые" лакказы (обзор) / Морозова О.В., Шумакович Г.П., Горбачева М.А. [и др.] // Биохимия. 2007. Т. 72. Стр. 1136-1150;

9. Purification and preliminary crystallographic study of Trametes versicolor laccase in its native form / Bertrand, T., Jolivalt, C., Caminade, E., [et al]. // Acta Cryst. 2002. V.58. P. 319-321;

10. Structure of native laccase from Trametes hirsuta at 1.8 A resolution / Polyakov K.M., Fedorova T.V., Stepanova E.V. // Acta Cryst. 2009. V. 65. P. 611-617;

11. Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: a review. / Durán N., Rosa M.A., D'Annibale A. [et al]. // Enzyme Microb Technol. 2002. V. 31. P. 907-31;

12. Лакказа-медиаторныесистемы и их использование (oбзор) / Морозова О.В., Шумакович Г.П., Шлеев С.В. [и др.] // Прикл. биохимия и микробиология. 2007. Т. 43. Стр. 583-597;

13. Morozova, O.V. «Blue» laccases / O.V. Morozova // Biochemistry. - 2007. - V. 72. - № 10. - P. 1136-1128;

14. Oxygen binding, activation, and reduction to water by copper proteins. / Solomon E.I., Chen P., Metz M. [et al]. // Angew Chem Int. Ed. 2001. V. 40. P. 4570-4590;

15. High power enzymatic biofuel cell based on naphthoquinone-mediatedoxidation of glucose by glucose oxidase in a carbon nanotube 3D matrix. / Reuillard B., Le Goff A., Agne`s C. [et al]. // Phys Chem. 2013. V. 15. P. 4892-4896;

16. Gold nanoparticles as electronic bridges for laccase-based biocathodes. / Gutie´rrez-Sa´nchez C., Pita M., Vaz-Domı´nguez C. [et al]. // J. Am. Chem. Soc. 2012. V. 134. P. 17212-17220;

17. Efficient direct oxygen reduction by laccases attached and oriented on pyrenefunctionalized polypyrrole/carbon nanotube electrodes. / Lalaoui N., Elouarzaki K., Le Goff A. et al. // Chem. Commun. 2013. V. 49. P. 9281-9283;

18. Improved chemical and physical stability of laccase after spherezyme immobilisation. / Jordaan J., Mathye S., Simpson C., Brady D. [et al]. // Enzyme Microb Technol. 2009. V. 45. N.432. P.5.

19. Application of eukaryotic and prokaryotic laccases in biosensor and biofuel cells: recent advances and electrochemical aspects. / Zhang, Y., Lv, Z., Zhou, J. [et al]. // Applied Microbiology and Biotechnology. 2018;

20. Bourbonnais, R., Paice, M.G. //FEBS. 1990. V. 267. P. 99-102;Fabbrini, M., Gall, i C., Gentili, P. //J. Mol. Catal. B: Enzym. 2002. V. 16. P. 231-240;

21. De Stefano L., Rea I., De Tommasi E., Rendina I., Rotiroti L., Giocondo M, et al. Bioactive modification of silicon surface using self-assembled hydrophobins from Pleurotus ostreatus. // Eur Phys J.E. 2009. V. 30. P. 181-5;

22. Silva C., Silva C.J., Zille A., Guebitz G.M., Cavaco-Paulo A. Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres. // Enzyme Microb Technol. 2007. V. 41. P. 867-75;

23. Arica M.Y., Altintas B., Bayramoglu G. Immobilization of laccase onto spacer-arm attached non-porouspoly (GMA/EGDMA) beads: application for textile dye degradation. // Bioresour Technol. 2009. V. 100. P. 665-9;

24. T. Beneyton, A. El Harrak, A.D. Griffiths. Immobilization of CotA, an extremophilic laccase from Bacillus subtilis, on glassy carbon electrodes for biofuel cell applications // Electrochemistry Communications 2011 V. 13 P.24-27;

25. Holzinger, M., Le Goff, A., and Cosnier, S. Carbon nanotube/enzyme biofuel cells. // Electrochim. Acta. 2012. V. 82. P. 179-190;

26. Blanford C.F., Heath R.S., Fraser A. A stable electrode for high-potential, electrocatalytic O2 reduction based on rational attachment of a blue copper oxidase to a graphite surface // Chem. Commun. 2007. P. 1710-1712;

27. C. Gutiérrez-Sánchez. Enhanced direct electron transfer between laccase and hierarchical carbon microfibers/carbon nanotubes composite electrodes. Comparison of three enzyme immobilization methods // Electrochimica Acta 2012. V. 82 P.218-223;

28. M. Bandapati, B. Krishnamurthy, S. Goel. Fully assembled Membraneless Glucose Biofuel Cell withMWCNT Modified Pencil Graphite leads as Novel Bioelectrodes. IEEE Trans Nano Bioscience 2019;

29. Laccase electrode for direct electrocatalytic reduction of O2 to H2O with high operational stability and resistance to chloride inhibition / Vaz-Dominguez C., Campuzano S., Rüdiger O. [et al]. // Biosens Bioelectron 2008. V. 24 P. 531-537;

30. G. Gupta, V. Rajendran, P. Atanassov. Bioelectrocatalysis of Oxygen Reduction Reaction by Laccase on Gold Electrodes // Electroanalysis 2004. V. 16 N. 13-14 P. 1182-1185;

31. Brady D., Jordaan J. Advances in enzyme immobilisation. // Biotechnol Lett. 2009. V. 31. P. 1639-50;

32. Rochefort D., Kouisni L., Gendron K. Physical immobilization of laccase on an electrode by means of poly(ethyleneimine) microcapsules. // J. Electroanal Chem. 2008. V. 617. P. 53-63;

33. Crestini C., Perazzini R., Saladino R. Oxidative functionalisation of lignin by layer-by layer immobilised laccases and laccase microcapsules. // Appl. Catal. Gen. 2010. V. 372. P. 115;

34. Jordaan J., Mathye S., Simpson C., Brady D. Improved chemical and physical stability of laccase after spherezyme immobilisation. // Enzyme Microb Technol. 2009. V. 45. N.432. P.5.