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.
|Original language||English (US)|
|Number of pages||13|
|Journal||Journal of Food Biochemistry|
|State||Published - Jul 1978|
All Science Journal Classification (ASJC) codes
- Food Science
- Cell Biology