Cationic effect of imidazolium-based ionic liquid on the stability of myoglobin |
| |
| Institution: | 1. School of Life Sciences, North Maharashtra University, Jalgaon, 425001, MS, India;2. G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia;1. Enzyme Technology and Protein Bioinformatics Laboratory, Department of Microbiology, Maharshi Dayanand University, Rohtak, 124001, Haryana, India;2. Division of Microbiology, Indian Agricultural Research Institute (IARI), New Delhi, India;3. Enzyme and Microbial Biochemistry Lab, Department of Chemistry, Indian Institute of Technology, Hauz-Khas, New Delhi 110016, India;1. Department of Chemical Engineering, Faculty of Sciences, University of Vigo (Campus Ourense), As Lagoas s/n, 32004 Ourense, Spain;2. Laboratory of Agro-food Biotechnology, CITI (University of Vigo)-Tecnópole, Parque Tecnológico de Galicia, San Cibrao das Viñas, 32900 Ourense, Spain;3. Bromatology Group, Department of Analytical and Food Chemistry, Faculty of Sciences, University of Vigo (Campus Ourense), As Lagoas s/n, 32004 Ourense, Spain;1. Department of Chemical Engineering and Food Engineering, Federal University of Santa Catarina (UFSC), Florianópolis, SC 88040-900, Brazil;2. Department of Pharmacy, Federal University of Sergipe (UFS), São Cristóvão, SE 49100-000, Brazil |
| |
| Abstract: | The conformational change of myoglobin (Mb) during guanidine hydrochloride (GuHCl)-induced protein unfolding in the presence of various ionic liquids (ILs) in phosphate buffer was investigated using both the Soret band absorption and the fluorescence of tryptophan measurements. The GuHCl-induced denaturation midpoints of Mb derived from the absorption and fluorescence spectra were almost similar in the presence of 150 mM ILs with the same cation 1-butyl-3-methylimidazolium (Bmim+) but different anions (BF4−, NO3−, Cl−, and Br−) in phosphate buffer. In addition, the denaturation midpoints of Mb in the presence of ILs were little lower than those in the absence of ILs in phosphate buffer. For the sake of clarity and comparison, we also measured the GuHCl-induced denaturation midpoints of Mb in the presence of 150 mM sodium salts with different anions (BF4−, NO3−, Cl−, and Br−) in phosphate buffer and found that their corresponding denaturation midpoints of Mb were almost similar to those observed in the absence of sodium salts in phosphate buffer. These experimental data indicate that Bmim+ cation can promote the unfolding of Mb. Further experiments revealed that the denaturation ability of ILs increases with increasing alkyl chain length of imidazolium cation of ILs and that hydroxyl-substituted imidazolium cation could also promote the unfolding of Mb. |
| |
| Keywords: | Myoglobin unfolding Guanidinium hydrochloride Ionic liquid Denaturation Absorption spectroscopy |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
