The use of enzymes in non-aqueous media is a technique that is now currently being investigated and commercially exploited. Here we report on the use of a novel immobilisation technique utilising an oil-in-water macroemulsion, termed a colloidal liquid aphron (CLA), to immobilise six different enzymes varying in molecular weight and pI. All enzymes were immobilised to a greater or lesser extent, with greater than 70% of beta-galactosidase and 90% of alpha-amylase effectively being immobilised over a wide range of pH values (4-10). It was found that in most cases pH had little effect on the degree of immobilisation. The method of immobilisation appeared to be related to the hydrophobicity and adiabatic compressibility of the enzyme, and its molecular weight. These enzymes also exhibited improved activity (superactivity) after immobilisation while the values of the Michaelis-Menten constant were altered. The major factor affecting loss of activity of the immobilised enzymes was found to be the anionic surfactant, sodium dodecyl sulphate, used in the polyaphron preparation. However SDS also appeared to enhance activity by altering protein conformation.