Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2016, Article ID 3647173, 7 pages
http://dx.doi.org/10.1155/2016/3647173
Research Article

Modification of the Sweetness and Stability of Sweet-Tasting Protein Monellin by Gene Mutation and Protein Engineering

1Department of Bioengineering, Qilu University of Technology, Jinan, Shandong 250353, China
2Department of Food Science and Engineering, Qilu University of Technology, Jinan, Shandong 250353, China

Received 1 October 2015; Revised 30 November 2015; Accepted 16 December 2015

Academic Editor: Shi-Jian Ding

Copyright © 2016 Qiulei Liu 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. J. A. Morris, R. Martenson, G. Deibler, and R. H. Cagan, “Characterization of monellin, a protein that tastes sweet,” The Journal of Biological Chemistry, vol. 248, no. 2, pp. 534–539, 1973. View at Google Scholar · View at Scopus
  2. T. Tancredi, H. Iijima, G. Saviano, P. Amodeo, and P. A. Temussi, “Structural determination of the active site of a sweet protein. A1H NMR investigation of pMNEI,” FEBS Letters, vol. 310, no. 1, pp. 27–30, 1992. View at Publisher · View at Google Scholar · View at Scopus
  3. M. Kohmura, N. Nio, and Y. Ariyoshi, “Complete amino acid sequence of the sweet protein monellin,” Agricultural and Biological Chemistry, vol. 54, no. 9, pp. 2219–2224, 1990. View at Publisher · View at Google Scholar · View at Scopus
  4. C. Ogata, M. Hatada, G. Tomlinson, W.-C. Shin, and S.-H. Kim, “Crystal structure of the intensely sweet protein monellin,” Nature, vol. 328, no. 6132, pp. 739–742, 1987. View at Google Scholar · View at Scopus
  5. J. R. Hobbs, S. D. Munger, and G. L. Conn, “Monellin (MNEI) at 1.15 Å resolution,” Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 63, no. 3, pp. 162–167, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Kohmura, N. Nio, and Y. Ariyoshi, “Solid-phase synthesis of crystalline monellin, a sweet protein,” Agricultural and Biological Chemistry, vol. 55, no. 2, pp. 539–545, 1991. View at Publisher · View at Google Scholar · View at Scopus
  7. W.-F. Xue, J. Carey, and S. Linse, “Multi-method global analysis of thermodynamics and kinetics in reconstitution of monellin,” Proteins: Structure, Function and Genetics, vol. 57, no. 3, pp. 586–595, 2004. View at Publisher · View at Google Scholar · View at Scopus
  8. S.-H. Kim, C.-H. Kang, R. Kim, J. M. Cho, Y.-B. Lee, and T.-K. Lee, “Redesigning a sweet protein: increased stability and renaturability,” Protein Engineering, vol. 2, no. 8, pp. 571–575, 1989. View at Publisher · View at Google Scholar · View at Scopus
  9. R. Spadaccini, O. Crescenzi, T. Tancredi et al., “Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin,” Journal of Molecular Biology, vol. 305, no. 3, pp. 505–514, 2001. View at Publisher · View at Google Scholar · View at Scopus
  10. Y.-H. Sung, J. Shin, H.-J. Chang, J. M. Cho, and W. Lee, “Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. Structural origin of sweetness,” The Journal of Biological Chemistry, vol. 276, no. 22, pp. 19624–19630, 2001. View at Publisher · View at Google Scholar · View at Scopus
  11. J. R. Somoza, J. M. Cho, and S.-H. Kim, “The taste-active regions of monellin, a potently sweet protein,” Chemical Senses, vol. 20, no. 1, pp. 61–68, 1995. View at Publisher · View at Google Scholar · View at Scopus
  12. V. Esposito, R. Gallucci, D. Picone, G. Saviano, T. Tancredi, and P. A. Temussi, “The importance of electrostatic potential in the interaction of sweet proteins with the sweet taste receptor,” Journal of Molecular Biology, vol. 360, no. 2, pp. 448–456, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. M. F. Rega, R. Di Monaco, S. Leone et al., “Design of sweet protein based sweeteners: hints from structure-function relationships,” Food Chemistry, vol. 173, pp. 1179–1186, 2015. View at Publisher · View at Google Scholar · View at Scopus
  14. S.-B. Lee, Y. Kim, J. Lee et al., “Stable expression of the sweet protein monellin variant MNEI in tobacco chloroplasts,” Plant Biotechnology Reports, vol. 6, no. 4, pp. 285–295, 2012. View at Publisher · View at Google Scholar · View at Scopus
  15. J. N. Brouwer, G. Hellekant, Y. Kasahara, H. van der Wel, and Y. Zotterman, “Electrophysiological study of the gustatory effects of the sweet proteins Monellin and Thaumatin in monkey, guinea pig and rat,” Acta Physiologica Scandinavica, vol. 89, no. 4, pp. 550–557, 1973. View at Publisher · View at Google Scholar · View at Scopus
  16. P. A. Temussi, “Sweet, bitter and umami receptors: a complex relationship,” Trends in Biochemical Sciences, vol. 34, no. 6, pp. 296–302, 2009. View at Publisher · View at Google Scholar · View at Scopus
  17. B. Liu, M. Ha, X.-Y. Meng et al., “Molecular mechanism of species-dependent sweet taste toward artificial sweeteners,” The Journal of Neuroscience, vol. 31, no. 30, pp. 11070–11076, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. B. Liu, M. Ha, X.-Y. Meng et al., “Functional characterization of the heterodimeric sweet taste receptor T1R2 and T1R3 from a New World monkey species (squirrel monkey) and its response to sweet-tasting proteins,” Biochemical and Biophysical Research Communications, vol. 427, no. 2, pp. 431–437, 2012. View at Publisher · View at Google Scholar · View at Scopus
  19. D. W. Bolen and G. D. Rose, “Structure and energetics of the hydrogen-bonded backbone in protein folding,” Annual Review of Biochemistry, vol. 77, pp. 339–362, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. K. A. Dill, “Dominant forces in protein folding,” Biochemistry, vol. 29, no. 31, pp. 7133–7155, 1990. View at Publisher · View at Google Scholar · View at Scopus
  21. W. Kauzmann, “Some factors in the interpretation of protein denaturation,” Advances in Protein Chemistry, vol. 14, pp. 1–63, 1959. View at Publisher · View at Google Scholar · View at Scopus
  22. C. Tanford, “Contribution of hydrophobic interactions to the stability of the globular conformation of proteins,” Journal of the American Chemical Society, vol. 84, no. 22, pp. 4240–4247, 1962. View at Publisher · View at Google Scholar · View at Scopus
  23. P. L. Privalov, “Stability of proteins: small globular proteins,” Advances in Protein Chemistry, vol. 33, pp. 167–241, 1979. View at Publisher · View at Google Scholar · View at Scopus
  24. C. M. Templeton, S. O. Pour, J. R. Hobbs, E. W. Blanch, S. D. Munger, and G. L. Conn, “Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix,” Chemical Senses, vol. 36, no. 5, pp. 425–434, 2011. View at Publisher · View at Google Scholar · View at Scopus
  25. W.-F. Xue, O. Szczepankiewicz, M. C. Bauer, E. Thulin, and S. Linse, “Intra-versus intermolecular interactions in monellin: contribution of surface charges to protein assembly,” Journal of Molecular Biology, vol. 358, no. 5, pp. 1244–1255, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. W.-F. Xue, O. Szczepankiewicz, E. Thulin, S. Linse, and J. Carey, “Role of protein surface charge in monellin sweetness,” Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics, vol. 1794, no. 3, pp. 410–420, 2009. View at Publisher · View at Google Scholar · View at Scopus
  27. O. Szczepankiewicz, C. Cabaleiro-Lago, G. G. Tartaglia et al., “Interactions in the native state of monellin, which play a protective role against aggregation,” Molecular BioSystems, vol. 7, no. 2, pp. 521–532, 2011. View at Publisher · View at Google Scholar · View at Scopus
  28. L. O'Brien, Alternative Sweeteners, Marcel Dekker, 3rd edition, 2001.
  29. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Publisher · View at Google Scholar · View at Scopus
  30. F. M. Assadi-Porter, D. J. Aceti, and J. L. Markley, “Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein,” Archives of Biochemistry and Biophysics, vol. 376, no. 2, pp. 259–265, 2000. View at Publisher · View at Google Scholar · View at Scopus
  31. R. Spadaccini, F. Trabucco, G. Saviano et al., “The mechanism of interaction of sweet proteins with the T1R2-T1R3 receptor: evidence from the solution structure of G16A-MNEI,” Journal of Molecular Biology, vol. 328, no. 3, pp. 683–692, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Aghera, I. Dasgupta, and J. B. Udgaonkar, “A buried ionizable residue destabilizes the native state and the transition state in the folding of monellin,” Biochemistry, vol. 51, no. 45, pp. 9058–9066, 2012. View at Publisher · View at Google Scholar · View at Scopus