DSC and FTIR Study of Adsorbed Lysozyme on Hydrophobic Surface
LEI Zu-meng1,GENG Xin-peng1*,DAI Li1,GENG Xin-du2
1. College of Environment & Chemical Engineering, Xi’an Polytechnic University, Xi’an 710048, China 2. Institute of Modern Separation Science, Northwest University, Xi’an 710069，China
Abstract：During a process of hen egg white lysozyme adsorption and folding on a moderately hydrophobic surface (PEG-600), the effects of salt((NH4)2SO4) concentrations, surface coverage and denaturant(guanidine hydrochloride,GuHCl) concentrations on thermal stability and the changes in the molecular conformation of adsorbed native and denatured lysozyme without aqueous solution were studied with a combination of differential scanning calorimetry (DSC) with FTIR spectroscopy. The results showed that temperature due to endothermic peaks was reduced and the disturbance increased at higher temperature with the increase in salt concentration and surface coverage of adsorbed protein. β-Sheet and β-Turn stucture increased while α-Helix structure decreased after the adsorption. The peaks corresponding to both C—C stretching frequency in 1 400-1 425 cm-1and amide I band frequency in 1 650-1 670 cm-1 of adsorbed denatured lysozyme can be detected in FTIR spectra while that due to amide I band frequency of adsorbed native lysozyme almost can’t be observed. Adsorption resulted in structural loss of adsorbed native lysozyme, whose performance was less stable.
雷祖猛1,耿信鹏1*,戴丽1,耿信笃2. 疏水表面上吸附态溶菌酶的DSC和FTIR研究[J]. 光谱学与光谱分析, 2008, 28(09): 2058-2061.
LEI Zu-meng1,GENG Xin-peng1*,DAI Li1,GENG Xin-du2. DSC and FTIR Study of Adsorbed Lysozyme on Hydrophobic Surface. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2008, 28(09): 2058-2061.
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