Protective effect of gemini surfactant on secondary structural change of bovine serum albumin in thermal denaturation up to 130 degrees C.

The effect of gemini surfactant, sodium dilauramidoglutamide lysine (DLGL), on the secondary structure of bovine serum albumin (BSA) was examined at 25 degrees C and at high temperatures up to 130 degrees C. The helicity (66%) of the protein decreased to 53% in the DLGL solution at 25 degrees C and it also decreased to 16% with rise of temperature. Although approximately half of the original helical structures were destroyed upon heating up to 75 degrees C, most of the structures were maximally protected in the coexistence of 0.