title: [DSC and FTIR study of adsorbed lysozyme on hydrophobic surface].
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. beta-Sheet and beta-Turn stucture increased while alpha-Helix structure decreased after the adsorption. The peaks corresponding to both C-C stretching frequency in 1400-1425 cm(-1) and amide I band frequency in 1650-1670 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.
authors.affiliation: College of Environment & Chemical Engineering, Xi'an Polytechnic University, Xi'an 710048, China.
authors.forename: Zu-meng
authors.initials: ZM
authors.lastname: Lei
authors.forename: Xin-peng
authors.initials: XP
authors.lastname: Geng
authors.forename: Li
authors.initials: L
authors.lastname: Dai
authors.forename: Xin-du
authors.initials: XD
authors.lastname: Geng
mesh_terms: D000327:Adsorption; D000818:Animals; D002152:Calorimetry, Differential Scanning; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties
chemical_list: C421864:hen egg lysozyme; D009113:Muramidase