# Dataset on the analysis of β-galactosidase immobilization efficiency on aminomethyl polystyrene (AMP) resin in syringe and column reactors

## TL;DR

This paper presents a dataset comparing how well β-galactosidase enzymes stick to and work in different reactor types for industrial use.

## Contribution

The dataset introduces detailed comparisons of β-galactosidase immobilization efficiency across multiple reactor types and methods.

## Key findings

- β-galactosidase was successfully immobilized on AMP resin using a PDC linker.
- Five approaches and reactor types were compared for immobilization efficiency and activity.
- The dataset supports industrial applications like lactose-free dairy production.

## 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.