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1. (WO2019026082) A RECOMBINANT FLAVIN-ADENINE DINUCLEOTIDE GLUCOSE DEHYDROGENASE AND USES THEREOF
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CLAIMS

1. A recombinant protein, comprising: (a) alpha subunit of an FAD-GDH; and (b) a minimal c-type cytochrome peptide.

2. The recombinant protein of claim 1, wherein said minimal c-type cytochrome peptide comprises 11 to 30 amino acids.

3. The recombinant protein of any one of claims 1 or 2, wherein said alpha subunit of an FAD-GDH is a Burkholderia cepacian alpha subunit of an FAD-GDH.

4. The recombinant protein of any one of claims 1 to 3, wherein said alpha subunit of an FAD-GDH is derived from a thermostable enzyme, an oxygen independent enzyme, or both.

5. The recombinant protein of any one of claims 1 to 4, wherein said minimal cytochrome peptide is a cytochrome domain MCR-2 from a MamP protein.

6. The recombinant protein of any one of claims 1 to 5, wherein said minimal cytochrome peptide is a magnetotactic bacterius minimal cytochrome peptide.

7. The recombinant protein of anyone of claims 1 to 6, having a molecular weight in the range of 63 to 65kDa.

8. The recombinant protein of anyone of claims 1 to 7, bound to a porphyrin comprising a metal.

9. The recombinant protein of anyone of claims 1 to 8, bound to a compound of formula I:


wherein said R is any electron donor, said compound of formula I is bound to a metal.

10. The recombinant protein of anyone of claims 8 or 9, wherein said metal is a trivalent metal or a divalent metal.

11. The recombinant protein of anyone of claims 8 to 10, having both peroxidase activity and oxidative activity.

12. The recombinant protein of any one of claims 1 to 11, comprising an amino acid sequence selected from the group consisting SED ID NOs: 8 to 13.

13. A composition comprising the recombinant protein any one of claims 1 to 12 and the gamma subunit of an FAD-GDH.

14. A composition comprising the recombinant protein any one of claims 1 to 12 and the gamma subunit of an FAD-GDH as two separate unbound proteins.

15. A DNA molecule comprising a nucleotide sequence encoding the recombinant protein of any one of claims 1 to 13 with or without the gamma subunit of an FAD-GDH.

16. The DNA molecule of claim 15, comprising the nucleic acid sequence selected from the group consisting SEQ ID NOs: 5-7 and 10.

17. An expression vector comprising the DNA molecule of any one of claims 15 or 16.

18. A cell comprising the DNA molecule of anyone of claims 16 or 17, the recombinant protein of any one of claims 1 to 12, or both.

19. The cell of claim 18, wherein said cell is a prokaryotic cell.

20. The recombinant protein of any one of claims 1 to 12, coupled to an electrode.

21. The recombinant protein of claim 20, wherein said coupled is covalently bound.

22. The recombinant protein of any one of claims 20 or 21, coupled to the an electrode via a mediator molecule comprising non-canonical amino acid (ncAA) residue.

23. An electrode coupled to a recombinant protein, the recombinant protein comprising:

(a) a cofactor of a redox enzyme;

(b) a redox enzyme;

(c) a linker moiety configured to link any one of: the cofactor or the enzyme to an electron transfer (ET) domain; and

(d) an ET domain configured to transfer electrons between the electrode and the cofactor; wherein a distance between said ET domain and the electrode is in the range of 0 to 14 A.

24. The electrode of claim 23, wherein the recombinant protein is in the form of formula: (a)-(b)-(c)-(d).

25. The electrode of claim 23, wherein the cofactor is selected from the group consisting of: FAD, NAD+, and NADP+.

26. The electrode of any one of claims 23 to 25, wherein the redox enzyme is selected from the group consisting of: oxidase, dehydrogenase, and malic enzyme.

27. The electrode of any one of claims 23 to 26, wherein the redox enzyme has a redox potential of less than 50 mV vs. Ag/AgCl.

28. The electrode of any one of claims 23 to 27, wherein the ET domain comprises a minimal c-type cytochrome peptide.

29. The electrode of any one of claims 23 to 28, comprising a material selected from gold, graphite, and glassy carbon electrode (GCE).

30. The electrode of any one of claims 23 to 29, wherein the ET is attached to the electrode.

31. The electrode of claim 30, wherein the ET is covalently attached to the electrode to the electrode via mediator molecule.

32. The electrode of claim 31, wherein said mediator molecule comprises one or more non-canonical amino acids.

33. The electrode of claim 32, wherein said one or more non-canonical amino acids comprise Propargyl -lysine (PrK).

34. The electrode of any one of claims 30 to 33, wherein said mediator molecule comprises polycyclic aromatic system.

35. A device comprising the electrode of any one of claims 23 to 34.

36. The device of claim 35, for biosensing glucose in a medium.

37. A method for determining an analyte in a liquid medium, the analyte being capable to undergo a biocatalytic oxidation or reduction reaction in the presence of an oxidizer or a reducer, respectively, the method comprising:

(i) providing the disclosed device in an embodiment thereof;

(ii) contacting the device with the liquid medium;

(iii) measuring the electric signal generated between the cathode and the anode, the electric signal being indicative of the presence and/or the concentration of the analyte; and

(iv) determining the analyte based on the electric signal.

38. The method of claim 37, wherein said analyte comprises glucose.

39. A method for transferring an electron to an electrode, comprising coupling the recombinant protein of any one of claims 1 to 12 to an electrode, thereby transferring an electron to said electrode.

40. The method of claim 39, wherein said coupling is in the absence of a mediator molecule.

41. A method for quantifying the amount of a reporter in a sample having a first detectable range of light absorbance in an oxidized state a second range of light absorbance in a non-oxidized state, comprising:

(a) contacting the recombinant protein of anyone of claims 1 to 12 with said reporter in a non-oxidized state; and

(b) measuring the amount of said reporter in an oxidized state,

thereby quantifying the amount of a reporter in a sample.

42. The method of claim 41, wherein said first detectable range of light absorbance is detectable in visible light and said second range of light absorbance is non-detectable in visible light.

43. The method of anyone of claims 41 or 42, wherein said reporter is 2,6-Dichloroindophenol.

44. The method of claim 43, wherein said 2,6-Dichloroindophenol is coupled to glucose.