Ultrasonic spectroscopy and differential scanning calorimetry of liposomal-encapsulated nisin

The thermal stability of phosphatidylcholine (PC) liposomes (colloidal dispersions of bilayer-forming polar lipids in aqueous solvents) in the presence and absence of the antimicrobial polypeptide nisin was evaluated using differential scanning calorimetry (DSC) and low-intensity ultrasonic spectroscopy (US). PC liposome mixtures with varying acyl chain lengths (C16:0 and C18:0) were formed in buffer with or without entrapped nisin. Gel-to-liquid crystalline phase transition temperatures (T-M) of liposomes determined from DSC thermograms were in excellent agreement with those determined by ultrasonic velocity and attenuation coefficient measurements recorded at 5 MHz. The dipalmitoylphosphatidylcholine (DPPC) T-M measured by DSC was similar to 41.3 and similar to 40.7 degrees C when measured by ultrasonic spectroscopy. The TM of distearoylphosphatidylcholine (DSPC) and DPPC/DSPC 1:1 liposomes was 54.3 and 54.9 degrees C and similar to 44.8 and similar to 47.3 degrees C when measured by DSC and US, respectively. The thermotropic stability generally increased upon addition of nisin. Analysis of the stepwise decrease in ultrasonic velocity with temperature indicated an increased compressibility corresponding to a loss of structure upon heating.