Biochem. Eng. J.

This paper reports our investigations on the secondary structure of lysozyme in aqueous solution with D2O and comparing systems emulsified with ionic and non-ionic amphiphiles, respectively. The opposite effect of concentration of surfactants on the lysozyme aqueous system was studied and the activity of lysozyme by the turbidimetric assay with different kinds of surfactant was compared. The effect of different surfactants on emulsification volume formed was observed and discussed. The different interactive patterns between lysozyme and ionic and non-ionic surfactants, such as sodium dodecyl sulfate (SDS), cetyl trimethyl ammonium bromide (CTAB) and Triton-X100 (Isooctoylphenoxypolyethoxy ethanol), respectively, was studied with FTIR. A simple relationship between the secondary structure and denaturation of protein is given for the emulsification of lysozyme in aqueous solutions. It is important for understanding the stabilization and avoiding the emulsions in the extraction process that the interactions between the proteins and surfactants which leads to the formation of such complexes are characterized. The utility of surfactants as a de-emulsifying agent for the commercial process to extract penicillin G from the filtrate of fermentation broth was consistent with these results. (C) 1998 Elsevier Science S.A. All rights reserved.This paper reports our investigations on the secondary structure of lysozyme in aqueous solution with D2O and comparing systems emulsified with ionic and non-ionic amphiphiles, respectively. The opposite effect of concentration of surfactants on the lysozyme aqueous system was studied and the activity of lysozyme by the turbidimetric assay with different kinds of surfactant was compared. The effect of different surfactants on emulsification volume formed was observed and discussed. The different interactive patterns between lysozyme and ionic and non-ionic surfactants, such as sodium dodecyl sulfate (SDS), cetyl trimethyl ammonium bromide (CTAB) and Triton-X100 (Isooctoylphenoxypolyethoxy ethanol), respectively, was studied with FTIR. A simple relationship between the secondary structure and denaturation of protein is given for the emulsification of lysozyme in aqueous solutions. It is important for understanding the stabilization and avoiding the emulsions in the extraction process that the interactions between the proteins and surfactants which leads to the formation of such complexes are characterized. The utility of surfactants as a de-emulsifying agent for the commercial process to extract penicillin G from the filtrate of fermentation broth was consistent with these results. (C) 1998 Elsevier Science S.A. All rights reserved