Abstract
Abstract The thermal denaturation of lysozymc in aqueous alcohol solution has been investigated by differential scanning calorimetry. The alcohols employed were methanol, ethanol, isomeric propyl alcohols and butyl alcohols as monohydric alcohols, and ethylene glycol and glycerol as polyhydric alcohols. In monohydric alcohols, the temperature of denaturation, Td, of lysozyme decreased linearly with increasing alcohol concentration, which became pronounced with an increasing in the hydrophobic character. The enthalpy of denaturation, ΔHd, of lysozyme showed a complex dependence on the solvent composition; the ΔHd first increased with increasing alcohol concentration and then started decreasing at different concentrations for each alcohol. The branching of the alkyl chain decreased the destabilizing effect of the alcohol on the native conformation of the protein. In polyhydric alcohols, both Td and ΔHd increased with increasing alcohol concentration. The polyhydric alcohols stabilized the native conformation of the protein in contrast with the monohydric alcohols. The results are discussed in terms of the hydrophobic and hydrophilic characters of the alcohols.
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.
