Abstract
Lysozyme crystals in the presence of 1-butyl-3-methylimidazolium tetrafluoroborate ([C4mim]BF4), 1-butyl-3-methylimidazolium chloride ([C4mim]Cl), 1-butyl-3-methylimidazolium bromide([C4mim]Br), and 1,3-dimethylimidazolium iodine([dmim]I) were prepared, and the influence of ionic liquids (ILs) on the structure and activity change of lysozyme was investigated. Fourier transform infrared spectroscopy revealed the major secondary structures of α-helix and β-sheet for lysozyme. It was interesting to note that increases of the band near 2,935 and 1,656 cm−1 from Raman spectroscopy are attributed to the unfolding of lysozyme molecules. A shift in amide III from 1,230 to 1,270 cm−1 in adding [dmim]I occurs, indicating a transformation from β-sheet to random coil. With regard to adding [C4mim]BF4, [C4mim]Cl, and [C4mim]Br, α-helix and β-sheet are the predominant structures for lysozyme. The activity study showed that the ILs used brought a positive effect. Especially, [dmim]I leads to a drastic increase in relative activity, and its value reaches 50 %.
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Liu, Y. D., Wu, G. Z., & Qi, M. Y. (2005). Polymorphous crystals from chlorozincate-choline chloride ionic liquids in different molar ratios. Journal in Crystal Growth, 281, 616–622.
Zhao, Y., Ma, C. Y., Yuan, S., & Philips, D. L. (2004). Study of succinylated food proteins by Raman spectroscopy. Journal of Agricultural and Food Chemistry, 52, 1815–1823.
Liu, W. N., Hou, Y. C., Wu, W. Z., Ren, S. H., Jing, Y., & Zhang, B. G. (2011). Solubility of glucose in ionic liquid t antisolvent mixtures. Industrial and Engineering Chemistry Research, 50, 6952–6956.
Pusey, M. L., Paley, M. S., Turner, M. B., & Rogers, R. D. (2007). Protein crystallization using room temperature ionic liquids. Crystal Growth and Design, 7, 787–793.
Judge, R. A., Takahashi, S., Longenecker, K. L., Fry, E. H., Abad-Zapatero, C., & Chiu, M. L. (2009). The effect of ionic liquids on protein crystallization and X-ray diffraction resolution. Crystal Growth and Design, 9, 3463–3469.
Lange, C., Patil, G., & Rudolph, R. (2005). Ionic liquids as refolding additives: N′-alkyl and N′-(omega-hydroxyalkyl) N-methylimidazolium chlorides. Protein Science, 14, 2693–2701.
Lu, J., Wang, X. J., & Ching, C. B. (2003). Effect of additives on the crystallization of lysozyme and chymotrypsinogen A. Crystal Growth and Design, 3, 83–87.
Kizel, R., Irudayaraj, J., & Seetharaman, K. (2002). Characterization of irradiated starches by using FT-Raman and FTIR spectroscopy. Journal of Agricultural and Food Chemistry, 50, 3912–3918.
Ma, C. Y., Rout, M. K., & Mock, W. Y. (2001). Study of oat globulin conformation by Fourier transform infrared spectroscopy. Journal of Agricultural and Food Chemistry, 49, 3328–3334.
Howell, N. K., Arteaga, G., & Nakai, S. (1999). Raman spectral analysis in the C–H stretching region of proteins and amino acids for investigation of hydrophobic interactions. Journal of Agricultural and Food Chemistry, 47, 924–933.
Herrero, A. M., Carmona, P., & Careche, M. (2004). Raman spectroscopic study of structural changes in hake (Merluccius merluccius L.) muscle proteins during frozen storage. Journal of Agricultural and Food Chemistry, 52, 2147–2153.
Alizadeh-pasdar, N., & Nakai, S. (2004). FT-Raman spectroscopy, fluorescent probe, and solvent accessibility study of egg and milk proteins. Journal of Agricultural and Food Chemistry, 52, 5277–5283.
Chakraborti, S., Chatterjee, T., Joshi, P., Poddar, A., Bhattacharyya, B., Singh, S. P., Gupta, V., & Chakrabarti, P. (2010). Structure and activity of lysozyme on binding to ZnO nanoparticles. Langmuir, 5, 3506–3513.
Nahar, S., & Tajmir-Riahi, H. A. (1996). Hg, Cd, and Pb with proteins of PSII: evidence for metal-sulfur binding and protein conformational transition by FTIR spectroscopy. Journal Colloid and Interface Science, 178, 648–656.
Macdonald, G. M., & Barry, B. A. (1992). Difference FT-IR study of a novel biochemical preparation of photosystem II. Biochemestry, 31, 9848–9856.
Chen, P., Tian, H. F., Zhang, L. N., & Chang, P. R. (2008). Structure and properties of soy protein plastics with ε-caprolactone/glycerol as binary plasticizers. Industrial Engineering Research, 47, 9389–9395.
Secundo, F., & Guerrieri, N. (2005). ATR-FT/IR study on the interactions between gliadins and dextrin and their effects on protein secondary structure. Journal of Agricultural and Food Chemistry, 53, 1757–1764.
Yang, X. Z., Wu, D. C., Du, Z. L., Li, R. X., Chen, X. L., & Li, X. H. (2009). Spectroscopy study on the interaction of quercetin with collagen. Journal of Agricultural and Food Chemistry, 57, 3431–3435.
Wang, Z. Z., Dang, L. P., & Jiang, P. P. (2010). Crystallization control of thermal stability and morphology of hen egg white lysozyme crystals by ionic liquids. Journal of Agricultural and Food Chemistry, 58, 5444–5448.
Byler, D. M., Farrell, H. M., & Susi, H. (1988). Raman spectroscopic study of casein structure. Journal of Dairy Science, 71, 2622–2629.
Lichan, E. C. Y. (1996). The application of Raman spectroscopy in food science. Trends in Food Science & Technology, 7, 361–370.
Ma, C. Y., Rout, M. K., Chan, W. M., & Phillips, D. L. (2000). Raman spectroscopic study of oat globulin conformation. Journal of Agricultural and Food Chemistry, 48, 1542–1547.
Meng, G., Ma, C. Y., & Phillips, D. L. (2003). Raman spectroscopic study of globulin from Phaseolus angularis (red bean). Food Chemistry, 81, 411–420.
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This work was funded by the National Natural Science Foundation of China (no. 20806053) and China Postdoctoral Science Foundation (no. 200902274).
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Dang, LP., Fang, WZ., Li, Y. et al. Ionic Liquid-Induced Structural and Activity Changes in Hen Egg White Lysozyme. Appl Biochem Biotechnol 169, 290–300 (2013). https://doi.org/10.1007/s12010-012-9986-z
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DOI: https://doi.org/10.1007/s12010-012-9986-z