Abstract
Abstract The interaction of a series of n-alkyl trimethyl ammonium bromides (C12, C14 and C16) with egg white lysozyme have been studied using fluorescence and UV-Vis spectroscopies and isothermal titration calorimetry (ITC). The trend of variation of molar absorptivity at 281 nm, quantum yields (λex=281 nm) and heat of interaction with respect to surfactant concentration, were measured. The spectrophotometric results show that the hydrophobic interactions have a major role in denaturation mechanism and it would be increased with increasing in hydrocarbon tail length of surfactant. The ITC results indicated the two-step mechanism for unfolding of lysozyme due to its interaction with surfactants.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
