Enhanced stability and reusability of alcohol dehydrogenase covalently immobilized on magnetic graphene oxide nanocomposites

Journal of Nanoscience and Nanotechnology

Volumn 15, Issue 2, 2015, Pages 1213-1220

  Liu, Liangliang ^a   Yu, Jingang ^a   Chen, Xiaoqing ^a  

^a CENTRAL SOUTH UNIVERSITY   (China)

Author keywords

Alcohol dehydrogenase; Graphene oxide; Immobilization; Magnetic

Indexed keywords

ENZYME IMMOBILIZATION; ENZYMES; FUNCTIONAL GROUPS; FUNCTIONAL MATERIALS; MAGNETIC SEPARATION; MAGNETIC STORAGE; NANOCOMPOSITES; NANOMAGNETICS; NANOPARTICLES; PH EFFECTS; RADIOACTIVE WASTE VITRIFICATION; REUSABILITY; STABILITY; SYNTHESIS (CHEMICAL);

ALCOHOL DEHYDROGENASE; COVALENT BINDING; ENHANCED STABILITY; GRAPHENE OXIDE NANOCOMPOSITES; GRAPHENE OXIDES; MAGNETIC; MICHAELIS CONSTANTS; STORAGE STABILITY;

GRAPHENE;

ALCOHOL DEHYDROGENASE; GRAPHITE; IMMOBILIZED ENZYME; MAGNETITE NANOPARTICLE; NANOCOMPOSITE; OXIDE;

ADSORPTION; CHEMISTRY; ENZYME ACTIVATION; ENZYME STABILITY; MATERIALS TESTING; PARTICLE SIZE; RECYCLING; SURFACE PROPERTY; ULTRASTRUCTURE;

ADSORPTION; ALCOHOL DEHYDROGENASE; ENZYME ACTIVATION; ENZYME STABILITY; ENZYMES, IMMOBILIZED; EQUIPMENT REUSE; GRAPHITE; MAGNETITE NANOPARTICLES; MATERIALS TESTING; NANOCOMPOSITES; OXIDES; PARTICLE SIZE; SURFACE PROPERTIES;

EID: 84920506844     PISSN: 15334880     EISSN: 15334899     Source Type: Journal    
DOI: 10.1166/jnn.2015.9024     Document Type: Article

References (39)

1. T. Li, F. Jia, Y. Fan, Z. Ding, and J. Yang, Biosens. Bioelectron. 42, 5 (2013).
2. R. Krishna, E. Titus, S. Chandra, N. K. Bardhan, R. Krishna, D. Bahadur, and J. Gracio, J. Nanosci. Nanotechno. 12, 6631 (2012).
3. W. Qin, Z. Song, C. Fan, W. Zhang, Y. Cai, Y. Zhang, and X. Qian, Anal. Chem. 84, 3138 (2012).
4. F. Xu, W. H. Wang, Y. J. Tan, and M. L. Bruening, Anal. Chem. 82, 10045 (2010).
5. D. Zhu, B. A. Hyatt, and L. Hua, J. Mol. Catal. B: Enzym. 56, 272 (2009).
6. B. Sahoo, S. K. Sahu, and P. Pramanik, J. Mol. Catal. B: Enzym. 69, 95 (2011).
7. C. López, S. D. Ríos, J. López-Santín, G. Caminal, and G. Álvaro, Biochem. Eng. J. 49, 414 (2010).
8. S. M. Robatjazi, S. A. Shojaosadati, R. Khalilzadeh, E. V. Farahani, and N. Balochi, Bioresource Technol. 104, 6 (2012).
9. D. A. Cowan and R. Fernandez-Lafuente, Enzyme Microb. Tech. 49, 326 (2011).
10. C. Mateo, J. M. Palomo, G. Fernandez-Lorente, J. M. Guisan, and R. Fernandez-Lafuente, Enzyme Microb. Tech. 40, 1451 (2007).
11. W. Bai, Y. J. Yang, X. Tao, J. F. Chen, and T. W. Tan, J. Mol. Catal. B: Enzym. 76, 82 (2012).
12. M. V. Kahraman, G. Bayramoolu, N. Kayaman-Apohan, and A. Güngör, Food Chem. 104, 1385 (2007).
13. Z. Yang, S. Si, H. Dai, and C. Zhang, Biosens. Bioelectron. 22, 3283 (2007).
14. Y. K. Chang and L. Chu, Biochem. Eng. J. 35, 37 (2007).
15. B. Krajewska, Enzyme Microb. Tech. 35, 126 (2004).
16. M. R. El-Aassar, J. Mol. Catal. B: Enzym. 85-86, 140 (2013).
17. L. Wang, R. Xu, Y. Chen, and R. Jiang, J. Mol. Catal. B: Enzym. 69, 120 (2011).
18. S. Thangavel, M. Elayaperumal, and G. Venugopal, Mater. Express 2, 327 (2012).
19. W. B. Yan, Y. Huang, Y. F. Xu, L. Huang, and Y. S. Chen, J. Nanosci. Nanotechno. 12, 2270 (2012).
20. K. Krishnamoorthy, N. Umasuthan, R. Mohan, J. Lee, and S. J. Kim, Sci. Adv. Mater. 4, 1111 (2012).
21. V. Tjoa, N. Mathews, J. Wei, and S. Mhaisalkar, Nanosci. Nanotech. Let. 4, 738 (2012).
22. L. Fan, C. Luo, M. Sun, X. Li, F. Lu, and H. Qiu, Bioresource Technol. 114, 703 (2012).
23. M. A. Khaderbad, V. Tjoa, N. Mathews, S. Madhu, M. Ravikanth, and V. R. Rao, Nanosci. Nanotech. Let. 4, 743 (2012).
24. M. Hasanzadeh and N. Shadjou, J. Nanosci. Nanotechno. 13, 4909 (2013).
25. Z. X. Liang, I. Tsigos, V. Bouriotis, and J. P. Klinman, J. Am. Chem. Soc. 126, 9500 (2004).
26. M. C. Madhusudhan, K. S. M. S. Raghavarao, and S. Nene, Biochem. Eng. J. 38, 414 (2008).
27. G. A. Petkova, K. Zaruba, and V. Kral, Bba-Proteins Proteom. 1824, 792 (2012).
28. Y. Liu, F. Yin, Y. Long, Z. Zhang, and S. Yao, J. Colloid Interf. Sci. 258, 75 (2003).
29. A. Trivedi, M. Heinemann, A. C. Spiess, T. Daussmann, and J. Büchs, J. Biosci. Bioeng. 99, 340 (2005).
30. Z. D. Zhou, G. Y. Li, and Y. J. Li, Int. J. Biol. Macromol. 47, 21 (2010).
31. A. S. Santos, A. C. Pereira, N. Durán, and L. T. Kubota, Electrochim. Acta 52, 215 (2006).
32. D. C. Marcano, D. V. Kosynkin, J. M. Berlin, A. Sinitskii, Z. Sun, A. Slesarev, L. B. Alemany, W. Lu, and J. M. Tour, Acs Nano 4, 4806 (2010).
33. Y. D. Li, H. Deng, X. L. Li, Q. Peng, X. Wang, and J. P. Chen, Angew. Chem. Int. Edit. 44, 2782 (2005).
34. M. M. Bradford, Anal. Biochem. 72, 248 (1976).
35. F. Bianchi, V. Chiesi, F. Casoli, P. Luches, L. Nasi, M. Careri, and A. Mangia, J. Chromatogr. A 1231, 8 (2012).
36. F. Wang, C. Guo, L. R. Yang, and C. Z. Liu, Bioresource Technol. 101, 8931 (2010).
37. L. Zhou, Y. Jiang, J. Gao, X. Zhao, L. Ma, and Q. Zhou, Biochem. Eng. J. 69, 28 (2012).
38. Y. Zhang, H. Wu, L. Li, J. Li, Z. Jiang, Y. Jiang, and Y. Chen, J. Mol. Catal. B: Enzym. 57, 130 (2009).
39. D. Li, W. Y. Teoh, J. J. Gooding, C. Selomulya, and R. Amal, Adv. Funct. Mater. 20, 1767 (2010).