ABSTRACT
This chapter describes the kinetic behavior of enzyme-loaded liposomes as can be observed from macroscopic measurements. Enzyme-loaded liposomes can be used as highly specific microreactors for exploiting the potential of enzymes in a variety of applications. Modeling enzyme-loaded liposomes may be helpful not only to estimate correctly the kinetic parameters from the experimental data or to compare experiments performed under different conditions, but also to design liposomes with the desired properties. Enzyme-liposome interactions can determine conformational changes in the protein structure and steric hindrances, whereas substrate–liposome interactions can give rise to partition effects and mass-transfer limitations. Steric hindrances are caused by the shielding effect of the liposomal membrane, which may reduce the accessibility to the substrate or effectors when the enzyme molecule interacts with the double layer. Partition effects are the result of hydrophobic and/or electrostatic interactions between the liposomal membrane and the components of the reaction medium.
