A strategy for efficient immobilization of laccase and horseradish peroxidase on single-walled carbon nanotubes

Journal of Chemical Technology and Biotechnology

Volumn 88, Issue 12, 2013, Pages 2227-2232

  Li, Ying ^a   Huang, Xirong ^a   Qu, Yinbo ^a  

^a SHANDONG UNIVERSITY   (China)

Author keywords

Carbon nanotube; Horseradish peroxidase; Immobilization; Laccase; Self assembly

Indexed keywords

ADSORPTION IMMOBILIZATION; CIRCULAR DICHROISM SPECTRA; ENZYMATIC PROPERTIES; ENZYME CONFORMATIONS; FLUORESCENCE SPECTRA; HORSE-RADISH PEROXIDASE; LACCASES; SINGLE-WALLED CARBON NANOTUBE (SWNTS);

ADSORPTION; CARBON NANOTUBES; CATALYTIC OXIDATION; RADIOACTIVE WASTE VITRIFICATION; SELF ASSEMBLY; SINGLE-WALLED CARBON NANOTUBES (SWCN);

ENZYME IMMOBILIZATION;

DIBENZOTHIOPHENE DERIVATIVE; HORSERADISH PEROXIDASE; IMMOBILIZED ENZYME; LACCASE; SINGLE WALLED NANOTUBE;

ADSORPTION; ARTICLE; CIRCULAR DICHROISM; ENZYME CONFORMATION; ENZYME IMMOBILIZATION; ENZYME MECHANISM; ENZYME SPECIFICITY; FLUORESCENCE SPECTROSCOPY; OXIDATION;

ARMORACIA RUSTICANA;

EID: 84887061999     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.4091     Document Type: Article

References (43)

1. Bachilo SM, Strano MS, Kittrell C, Hauge RH, Smalley RE and Weisman RB, Structure-assigned optical spectra of single-walled carbon nanotubes. Science 298:2361-2366 (2002).
2. Iijima S, Helical microtubules of graphitic carbon. Nature 354:56-58 (1991).
3. Iijima S and Ichihashi T, Single-shell carbon nanotubes of 1-nm diameter. Nature 363:603-605 (1993).
4. Strano MS, Dyke CA, Usrey ML, Barone PW, Allen MJ, Shan H, Kittrell C, Hauge RH, Tour JM and Smalley RE, Electronic structure control of single-walled carbon nanotube functionalization. Science 301:1519-1522 (2003).
5. Cella LN, Chen W, Myung NV and Mulchandani A, Single-walled carbon nanotube-based chemiresistive affinity biosensors for small molecules: ultrasensitive glucose detection. J Am Chem Soc 132:5024-5026 (2010).
6. Kim KH, Oh Y and Islam MF, Graphene coating makes carbon nanotube aerogels superelastic and resistant to fatigue. Nat Nanotechnol 7:562-566 (2012).
7. Valcarcel M, Cardenas S and Simonet BM, Role of carbon nanotubes in analytical science. Anal Chem 79:4788-4797 (2007).
8. Wang H, Wu Z, Plaseied A, Jenkins P, Simpson L, Engtrakul C and Ren Z, Carbon nanotube modified air-cathodes for electricity production in microbial fuel cells. J Power Sources 196:7465-7469 (2011).
9. Zhu Z, Garcia-Gancedo L, Flewitt AJ, Moussy F, Li Y and Milne WI, Design of carbon nanotube fiber microelectrode for glucose biosensing. J Chem Technol Biotechnol 87:256-262 (2012).
10. Das D and Das PK, Superior activity of structurally deprived enzyme-carbon nanotube hybrids in cationic reverse micelles. Langmuir 25:4421-4428 (2009).
11. Moore VC, Strano MS, Haroz EH, Hauge RH, Smalley RE, Schmidt J and Talmon Y, Individually suspended single-walled carbon nanotubes in various surfactants. Nano Lett 3:1379-1382 (2003).
12. Zhong W and Claverie JP, Probing the carbon nanotube-surfactant interaction for the preparation of composites. Carbon 51:72-84 (2013).
13. Grunlan JC, Liu L and Kim YS, Tunable single-walled carbon nanotube microstructure in the liquid and solid states using poly (acrylic acid). Nano Lett 6:911-915 (2006).
14. Nap R and Szleifer I, Control of carbon nanotube-surface interactions: the role of grafted polymers. Langmuir 21:12072-12075 (2005).
15. Cathcart H, Nicolosi V, Hughes JM, Blau WJ, Kelly JM, Quinn SJ and Coleman JN, Ordered DNA wrapping switches on luminescence in single-walled nanotube dispersions. J Am Chem Soc 130:12734-12744 (2008).
16. Zheng M, Structure-based carbon nanotube sorting by sequence-dependent DNA assembly. Science 302:1545-1548 (2003).
17. Karajanagi SS, Yang H, Asuri P, Sellitto E, Dordick JS and Kane RS, Protein-assisted solubilization of single-walled carbon nanotubes. Langmuir 22:1392-1395 (2006).
18. Nakashima N, Okuzono S, Murakami H, Nakai T and Yoshikawa K, DNA dissolves single-walled carbon nanotubes in water. Chem Lett 32:456-457 (2003).
19. Nie H, Wang H, Cao A, Shi Z, Yang S-T, Yuan Y and Liu Y, Diameter-selective dispersion of double-walled carbon nanotubes by lysozyme. Nanoscale 3:970-973 (2011).
20. Karajanagi SS, Vertegel AA, Kane RS and Dordick JS, Structure and function of enzymes adsorbed onto single-walled carbon nanotubes. Langmuir 20:11594-11599 (2004).
21. Asuri P, Bale SS, Pangule RC, Shah DA, Kane RS and Dordick JS, Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes. Langmuir 23:12318-12321 (2007).
22. Crespilho FN, Emilia Ghica M, Florescu M, Nart FC, Oliveira ON and Brett C, A strategy for enzyme immobilization on layer-by-layer dendrimer-gold nanoparticle electrocatalytic membrane incorporating redox mediator. Electrochem Commun 8:1665-1670 (2006).
23. Tu X, Zhao Y, Luo S, Luo X and Feng L, Direct electrochemical sensing of glucose using glucose oxidase immobilized on functionalized carbon nanotubes via a novel metal chelate-based affinity method. Microchim Acta:1-8 (2012). Is there a volume number?
24. Sassolas A, Blum LJ and Leca-Bouvier BD, Immobilization strategies to develop enzymatic biosensors. Biotechnol Adv 30:489-511 (2012).
25. Becker JW, Reeke GN, Jr., Cunningham BA and Edelman GM, New evidence on the location of the saccharide-binding site of concanavalin A. Nature 259:406-409 (1976).
26. Matto M and Husain Q, Entrapment of porous and stable concanavalin A-peroxidase complex into hybrid calcium alginate-pectin gel. J Chem Technol Biotechnol 81:1316-1323 (2006).
27. Xue Y, Ding L, Lei J, Yan F and Ju H, In situ electrochemical imaging of membrane glycan expression on micropatterned adherent single cells. Anal Chem 82:7112-7118 (2010).
28. Qiu H, Lu L, Huang X, Zhang Z and Qu Y, Immobilization of horseradish peroxidase on nanoporous copper and its potential applications. Bioresource Technol 101:9415-9420 (2010).
29. --type ionic liquids on direct electrochemistry and electrocatalysis of horseradish peroxidase in Nafion films. Colloid Surface B 87:61-66 (2011).
30. 2 biofuel cell. Electrochem Commun 9:331-336 (2007).
31. Liu Y, Qu X, Guo H, Chen H, Liu B and Dong S, Facile preparation of amperometric laccase biosensor with multifunction based on the matrix of carbon nanotubes-chitosan composite. Biosens Bioelectron 21:2195-2201 (2006).
32. 2-electroreduction biocatalyst superior to platinum and a biofuel cell operating at 0.88 V. J Am Chem Soc 126:8368-8369 (2004).
33. Xue L, Qiu H, Li Y, Lu L, Huang X and Qu Y, A novel water-in-ionic liquid microemulsion and its interfacial effect on the activity of laccase. Colloid Surface B 82:432-437 (2011).
34. Jia W, Jin C, Xia W, Muhler M, Schuhmann W and Stoica L, Glucose oxidase/horseradish peroxidase Co-immobilized at a CNT-modified graphite electrode: towards potentially implantable biocathodes. Chem - Eur J 18:2783-2786 (2012).
35. Qiu H, Xu C, Huang X, Ding Y, Qu Y and Gao P, Adsorption of laccase on the surface of nanoporous gold and the direct electron transfer between them. J Phys Chem C 112:14781-14785 (2008).
36. Qiu H, Xu C, Huang X, Ding Y, Qu Y and Gao P, Immobilization of laccase on nanoporous gold: comparative studies on the immobilization strategies and the particle size effects. J Phys Chem C 113:2521-2525 (2009).
37. Li C, Jiang Z, Gao J, Yang Y, Wang S, Tian F, Sun F, Sun X, Ying P and Han C, Ultra-deep desulfurization of diesel: oxidation with a recoverable catalyst assembled in emulsion. Chem - Eur J 10:2277-2280 (2004).
38. Sachdeva T and Pant K, Deep desulfurization of diesel via peroxide oxidation using phosphotungstic acid as phase transfer catalyst. Fuel Process Technol 91:1133-1138 (2010).
39. Montiel C, Terrés E, Domínguez JM and Aburto J, Immobilization of chloroperoxidase on silica-based materials for 4, 6-dimethyl dibenzothiophene oxidation. J Mol Catal B: Enzyme 48:90-98 (2007).
40. Bradford MM, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254 (1976).
41. Bucur B, Danet AF and Marty J-L, Versatile method of cholinesterase immobilisation via affinity bonds using Concanavalin A applied to the construction of a screen-printed biosensor. Biosens Bioelectron 20:217-225 (2004).
42. Gajhede M, Schuller DJ, Henriksen A, Smith AT and Poulos TL, Crystal structure of horseradish peroxidase C at 2.15 resolution. Nat Struct Mol Biol 4:1032-1038 (1997).
43. Ren L, Yan D and Zhong W, Enhanced enzyme activity through electron transfer between single-walled carbon nanotubes and horseradish peroxidase. Carbon 50:1303-1310 (2012).