Abstract
The effect of both lipid headgroup charge and of aqueous subphase pH on adsorption of glucose oxidase molecules (GOx) into dibehenoylphosphatidylcholine (DBPC) and octadecylamine (ODA) monolayers has been studied by surface tension and surface pressure measurements. The results revealed that whereas the extent of GOx adsorption into pure DBPC monolayers essentially depended on the area in a monolayer available to harbor adsorbing GOx molecules, enhanced enzyme penetration into a monolayer occurred at high surface densities. The kinetics of enzyme penetration was found to be dependent of the initial surface pressure of a spread monolayer. The addition of ODA to DBPC monolayers gave a dramatic boost to GOx penetration and at high molecular surface densities largely depended on the ratio of ODA in the mixed monolayers. This increase in GOx penetration was attributed to the strong attractive electrostatic interaction between the positively charged ODA and the negatively charged enzyme.
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