Abstract
β-Galactosidase was covalently immobilized on AMP resin using a p-phenylenediisothiocyanate (PDC) linker. Resin loading was determined by measuring the protein concentration difference between the original lactase solution and the reactor supernatant using a Bradford assay. Enzyme activity of the supernatants was assessed with ONPG as the substrate, and lactose turnover rates were measured using a lactose solution. The dataset provides detailed results for five different approaches with several syringe reactors and two column reactors, enabling comparison of immobilization efficiency and catalytic performance. The dataset may be valuable for industrial applications where stable and efficient immobilized β-galactosidase systems are required, such as lactose-free dairy production.