title: Analysis of claims of enhanced enzyme catalysis by inorganic colloidosomes.
abstract: Ester hydrolysis reactions in the presence of enzymes have been reported to occur within inorganic colloidsomes that contain water in organic solvents. Analysis of reported data plots that were used to obtain values for Km and Vmax that led to those conclusions show that there is a linear dependence of the initial rates on the concentration of substrate, with no evidence of saturation that is necessary to establish binding of reactants and enzymes. The results do establish that there is no Michaelis-Menten complex formed between the substrates and enzymes. Therefore, any calculations of enzyme kinetic parameters from these data and the resulting conclusions should be reconsidered.
authors.forename: Ronald
authors.initials: R
authors.lastname: Kluger
keywords: Colloidosomes; Ester hydrolysis; Inverse plot; Organic solvent; Saturation