Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2017, Article ID 5031809, 8 pages
https://doi.org/10.1155/2017/5031809
Research Article

Online Detection of Peroxidase Using 3D Printing, Active Magnetic Mixing, and Spectra Analysis

1Key Laboratory of Agricultural Information Acquisition Technology (Beijing), Ministry of Agriculture, China Agricultural University, Beijing, China
2College of Veterinary Medicine, China Agricultural University, Beijing, China
3Hebei Animal Disease Control Center, Shijiazhuang, China
4Modern Precision Agriculture System Integration Research Key Laboratory of Ministry of Education, China Agricultural University, Beijing, China

Correspondence should be addressed to Jianhan Lin; nc.ude.uac@nahnaij

Received 13 October 2016; Revised 16 February 2017; Accepted 3 April 2017; Published 24 April 2017

Academic Editor: András Fodor

Copyright © 2017 Shanshan Bai et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. K. W. A. Westman, D. Selga, P. Bygren et al., “Clinical evaluation of a capture ELISA for detection of proteinase-3 antineutrophil cytoplasmic antibody,” Kidney International, vol. 53, no. 5, pp. 1230–1236, 1998. View at Publisher · View at Google Scholar · View at Scopus
  2. J. Yang, X. Dai, H. Chen et al., “Development of blocking ELISA for detection of antibodies against H9N2 avian influenza viruses,” Journal of Virological Methods, vol. 229, pp. 40–47, 2016. View at Publisher · View at Google Scholar · View at Scopus
  3. S. Mao, X. Ou, D. Zhu et al., “Development and evaluation of indirect ELISAs for the detection of IgG, IgM and IgA1 against duck hepatitis A virus 1,” Journal of Virological Methods, vol. 237, pp. 79–85, 2016. View at Publisher · View at Google Scholar
  4. L. Zhu, J. He, X. Cao, K. Huang, Y. Luo, and W. Xu, “Development of a double-antibody sandwich ELISA for rapid detection of Bacillus Cereus in food,” Scientific Reports, vol. 6, Article ID 16092, 2016. View at Publisher · View at Google Scholar · View at Scopus
  5. B. K. Van Weemen and A. H. W. M. Schuurs, “Immunoassay using antigen-enzyme conjugates,” FEBS Letters, vol. 15, no. 3, pp. 232–236, 1971. View at Publisher · View at Google Scholar · View at Scopus
  6. E. Engvall and P. Perlmann, “Enzyme-linked immunosorbent assay (ELISA) quantitative assay of immunoglobulin G,” Immunochemistry, vol. 8, no. 9, pp. 871–874, 1971. View at Publisher · View at Google Scholar · View at Scopus
  7. M. F. Clark and A. N. Adams, “Characteristics of the microplate method of enzyme linked immunosorbent assay for the detection of plant viruses,” Journal of General Virology, vol. 34, no. 3, pp. 475–483, 1977. View at Publisher · View at Google Scholar · View at Scopus
  8. S. Z. Huang, Y. Z. Du, and Y. H. Zhang, “Establishment and application of ELISA method for detecting Salmonella SPP,” Chinese Journal of Preventive Veterinary Medicine, vol. 28, no. 2, pp. 196–200, 2006. View at Google Scholar
  9. P. S. Holt, R. K. Gast, and C. R. Greene, “Rapid detection of Salmonella enteritidis in pooled liquid egg samples using a magnetic bead-ELISA system,” Journal of Food Protection, vol. 58, no. 9, pp. 967–972, 1995. View at Publisher · View at Google Scholar · View at Scopus
  10. R. Kumar, P. K. Surendran, and N. Thampuran, “Evaluation of culture, ELISA and PCR assays for the detection of Salmonella in seafood,” Letters in Applied Microbiology, vol. 46, no. 2, pp. 221–226, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. L. Ji, J. Liu, C. Qian, and X. Chen, “Advances in the application of urea-hydrogen peroxide to oxidation reactions,” Chinese Journal of Organic Chemistry, vol. 32, no. 2, pp. 254–265, 2012. View at Publisher · View at Google Scholar · View at Scopus
  12. K. Chattopadhyay and S. Mazumdar, “Structural and conformational stability of horseradish peroxidase: effect of temperature and pH,” Biochemistry, vol. 39, no. 1, pp. 263–270, 2000. View at Publisher · View at Google Scholar · View at Scopus
  13. B. Ibarlucea, X. Munoz-Berbel, P. Ortiz, S. Büttgenbach, C. Fernández-Sánchez, and A. Llobera, “Self-validating lab-on-a-chip for monitoring enzyme-catalyzed biological reactions,” Sensors and Actuators B: Chemical, vol. 237, pp. 16–23, 2016. View at Publisher · View at Google Scholar · View at Scopus
  14. I. Rodríguez-Ruiz, E. Masvidal-Codina, T. N. Ackermann, and A. Llobera, “Photonic lab-on-chip (PhLOC) for enzyme-catalyzed reactions in continuous flow,” Microfluidics and Nanofluidics, vol. 18, no. 5-6, pp. 1277–1286, 2015. View at Publisher · View at Google Scholar · View at Scopus
  15. R. Davidsson, B. Johansson, V. Passoth, M. Bengtsson, T. Laurell, and J. Emnéus, “Microfluidic biosensing systems Part II. Monitoring the dynamic production of glucose and ethanol from microchip-immobilised yeast cells using enzymatic chemiluminescent μ-biosensors,” Lab on a Chip—Miniaturisation for Chemistry and Biology, vol. 4, no. 5, pp. 488–494, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. M. A. Ansari, K.-Y. Kim, K. Anwar, and S. M. Kim, “Vortex micro T-mixer with non-aligned inputs,” Chemical Engineering Journal, vol. 181-182, no. 1, pp. 846–850, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. J. J. Chen, C. H. Chen, and S. R. Shie, “Interfacial configurations and mixing performances of fluids in staggered curved-channel micromixers,” in Proceedings of the Symposium on Design, Test, Integration and Packaging of Mems/Moems, pp. 170–175, May 2011.
  18. B. Eickenberg, F. Wittbracht, P. Stohmann et al., “Continuous-flow particle guiding based on dipolar coupled magnetic superstructures in rotating magnetic fields,” Lab on a Chip, vol. 13, no. 5, pp. 920–927, 2013. View at Publisher · View at Google Scholar · View at Scopus
  19. H. E. H. Meijer, M. K. Singh, T. G. Kang, J. M. J. Den Toonder, and P. D. Anderson, “Passive and active mixing in microfluidic devices,” Macromolecular Symposia, vol. 279, no. 1, pp. 201–209, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. J. C. McDonald, D. C. Duffy, J. R. Anderson et al., “Fabrication of microfluidic systems in poly(dimethylsiloxane),” Electrophoresis, vol. 21, no. 1, pp. 27–40, 2000. View at Publisher · View at Google Scholar · View at Scopus
  21. A. Alam and K.-Y. Kim, “Mixing performance of a planar micromixer with circular chambers and crossing constriction channels,” Sensors and Actuators B: Chemical, vol. 176, no. 1, pp. 639–652, 2013. View at Publisher · View at Google Scholar · View at Scopus
  22. M. A. Ansari and K.-Y. Kim, “Mixing performance of unbalanced split and recombine micomixers with circular and rhombic sub-channels,” Chemical Engineering Journal, vol. 162, no. 2, pp. 760–767, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. N. L. Jeon, D. T. Chiu, C. J. Wargo et al., “Design and fabrication of integrated passive valves and pumps for flexible polymer 3-dimensional microfluidic systems,” Biomedical Microdevices, vol. 4, no. 2, pp. 117–121, 2002. View at Publisher · View at Google Scholar · View at Scopus
  24. R. Y. Neches, K. J. Flynn, L. Zaman, E. Tung, and N. Pudlo, “On the intrinsic sterility of 3D printing,” PeerJ, vol. 4, Article ID e2661, 2016. View at Publisher · View at Google Scholar
  25. G. Comina, A. Suska, and D. Filippini, “PDMS lab-on-a-chip fabrication using 3D printed templates,” Lab on a Chip, vol. 14, no. 2, pp. 424–430, 2014. View at Publisher · View at Google Scholar · View at Scopus
  26. V. Sanz, S. de Marcos, and J. Galbán, “A reagentless optical biosensor based on the intrinsic absorption properties of peroxidase,” Biosensors and Bioelectronics, vol. 22, no. 6, pp. 956–964, 2007. View at Publisher · View at Google Scholar · View at Scopus
  27. M. J. Rodriguez Maranon, D. Mercier, R. B. Van Huystee, and M. J. Stillman, “Analysis of the optical absorption and magnetic-circular-dichroism spectra of peanut peroxidase: electronic structure of a peroxidase with biochemical properties similar to those of horseradish peroxidase,” Biochemical Journal, vol. 301, no. 2, pp. 335–341, 1994. View at Publisher · View at Google Scholar · View at Scopus