Table of Contents
ISRN Biotechnology
Volume 2013, Article ID 737805, 7 pages
http://dx.doi.org/10.5402/2013/737805
Research Article

Macromolecular Crowding Enhances Catalytic Efficiency and Stability of α-Amylase

1Department of Protein Chemistry and Technology, Central Food Technological Research Institute, Mysore 570 020, India
2Max-Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany

Received 20 June 2012; Accepted 13 August 2012

Academic Editors: E. Formentin and J. Sereikaite

Copyright © 2013 Jay Kant Yadav. 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. W. Wang, “Protein aggregation and its inhibition in biopharmaceutics,” International Journal of Pharmaceutics, vol. 289, no. 1-2, pp. 1–30, 2005. View at Publisher · View at Google Scholar · View at Scopus
  2. L. L. Chang, D. Shepherd, J. Sun et al., “Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?” Journal of Pharmaceutical Sciences, vol. 94, no. 7, pp. 1427–1444, 2005. View at Publisher · View at Google Scholar · View at Scopus
  3. V. Ragoonanan and A. Aksan, “Protein stabilization,” Transfusion Medicine and Hemotherapy, vol. 34, no. 4, pp. 246–252, 2007. View at Publisher · View at Google Scholar · View at Scopus
  4. Y. Fujita, Y. Iwasa, and Y. Noda, “Effect of polyhydric alcohols on invertase stabilization,” Bulletin of the Chemical Society of Japan, vol. 55, pp. 1896–1900, 1984. View at Google Scholar
  5. K. Gekko, “Calorimetric study on thermal denaturation of lysozyme in polyol-water mixtures,” Journal of Biochemistry, vol. 91, no. 4, pp. 1197–1204, 1982. View at Google Scholar · View at Scopus
  6. T. Arakawa and S. N. Timasheff, “Preferential interactions of proteins with salts in concentrated solutions,” Biochemistry, vol. 21, no. 25, pp. 6545–6552, 1982. View at Google Scholar · View at Scopus
  7. S. N. Timasheff, “The control of protein stability and association by weak interactions with water: how do solvents affect these processes?” Annual Review of Biophysics and Biomolecular Structure, vol. 22, pp. 67–97, 1993. View at Google Scholar · View at Scopus
  8. M. B. Burg and J. D. Ferraris, “Intracellular organic osmolytes: function and regulation,” The Journal of Biological Chemistry, vol. 283, no. 12, pp. 7309–7313, 2008. View at Publisher · View at Google Scholar · View at Scopus
  9. O. Bounedjah, L. Hamon, P. Savarin, B. Desforges, Curmi, and D. Pastre, “Macromolecular crowding regulates assembly of mRNA stress granules after osmotic stress,” The Journal of Biological Chemistry, vol. 287, pp. 2446–2458, 2012. View at Google Scholar
  10. L. Hamon, P. Savarin, P. A. Curmi, and D. Pastre, “Rapid assembly and collective behavior of microtubule bundles in the presence of polyamines,” Biophysical Journal, vol. 101, pp. 205–216, 2011. View at Google Scholar
  11. S. B. Zimmerman and S. O. Trach, “Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli,” Journal of Molecular Biology, vol. 222, no. 3, pp. 599–620, 1991. View at Google Scholar · View at Scopus
  12. G. K. Farber and G. A. Petsko, “The evolution of α/β barrel enzymes,” Trends in Biochemical Sciences, vol. 15, no. 6, pp. 228–234, 1990. View at Google Scholar · View at Scopus
  13. S. Janecek, “Alpha-amylase family: molecular biology and evolution,” Progress in Biophysics and Molecular Biology, vol. 67, pp. 67–97, 1997. View at Google Scholar
  14. E. A. MacGregor, “α-Amylase structure and activity,” Journal of Protein Chemistry, vol. 7, no. 4, pp. 399–415, 1988. View at Google Scholar · View at Scopus
  15. L. Holm, A. K. Koivula, P. M. Lehtovaara, A. Hemminki, and J. K. C. Knowles, “Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus alpha-amylase,” Protein Engineering, vol. 3, no. 3, pp. 181–191, 1990. View at Google Scholar · View at Scopus
  16. O. H. Lowry, N. J. Rosenbrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951. View at Google Scholar · View at Scopus
  17. P. Bernfeld, “α- and β-Amylases,” Methods in Enzymology, vol. 1, pp. 149–158, 1955. View at Publisher · View at Google Scholar · View at Scopus
  18. N. Declerck, M. Machius, P. Joyet, G. Wiegand, R. Huber, and C. Gaillardin, “Hyperthermostabilization of Bacillus licheniformisα-amylase and modulation of its stability over a 50°C temperature range,” Protein Engineering, vol. 16, no. 4, pp. 287–293, 2003. View at Google Scholar · View at Scopus
  19. J. C. Lee and S. N. Timasheff, “The stabilization of proteins by sucrose,” The Journal of Biological Chemistry, vol. 256, no. 14, pp. 7193–7201, 1981. View at Google Scholar · View at Scopus
  20. S. Rajendran, C. Radha, and V. Prakash, “Mechanism of solvent-induced thermal stabilization of α-amylase from Bacillus amyloliquefaciens,” International Journal of Peptide and Protein Research, vol. 45, no. 2, pp. 122–128, 1995. View at Google Scholar · View at Scopus
  21. S. N. Timasheff, “Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated,” Advances in Protein Chemistry, vol. 51, pp. 355–432, 1998. View at Google Scholar · View at Scopus
  22. R. Santucci, F. Polizio, and A. Desideri, “Formation of a molten-globule-like state of cytochrome c induced by high concentrations of glycerol,” Biochimie, vol. 81, no. 7, pp. 745–750, 1999. View at Publisher · View at Google Scholar · View at Scopus
  23. J. K. Yadav and V. Prakash, “Thermal stability of alpha-amylase in aqueous cosolvent systems,” Journal of Biosciences, vol. 34, no. 3, pp. 377–387, 2009. View at Google Scholar · View at Scopus
  24. S. N. Timasheff, “Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 15, pp. 9721–9726, 2002. View at Publisher · View at Google Scholar · View at Scopus
  25. S. N. Timasheff, “Protein hydration, thermodynamic binding, and preferential hydration,” Biochemistry, vol. 41, no. 46, pp. 13473–13482, 2002. View at Publisher · View at Google Scholar · View at Scopus