THE KINETIC PROPERTIES OF LACTASE, PAPAIN AND LIPASE IMMOBILIZED ON A SINGLE SUPPORT

Lactase, papain and lipase enzymes were immobilized concomitantly on derivatized Sepharose 4‐B. Equal molar concentrations of each enzyme were allowed to react with activated Sepharose and a preferential binding of lipase and papain over lactase was observed. This preferential binding was explained by differences in diffusion rates of enzymes resulting in greater availability of binding sites within the beads to certain enzyme species. The effects of pH of assay, temperature of assay and substrate concentrations on each individual enzyme were determined. Soluble forms of each enzyme were used for comparison. There were some differences in pH and temperature optima for the immobilized enzymes. However, the affinity of the enzymes for their substrates was substantially the same.