Supplementary material for immobilized beta-glucosidase

This dataset supports the study on the development of a robust and eco-friendly biocatalyst based on thermostable β-glucosidase immobilized on linen fabric. The β-glucosidase enzyme was immobilized using a covalent periodate-based method, with ethylenediamine-glutaraldehyde as a spacer to enhance performance. Two biocatalyst systems were developed and tested (Lf-β-glucosidase and LfEG-β-glucosidase). This dataset supports the study on the characterization of thermostable β-glucosidase immobilized on linen fabric for sustainable lactose hydrolysis and whey valorization. The supplementary materials include figures and tables related to enzyme purification and kinetic analysis. Supplementary Figure 1 presents the results of nickel affinity chromatography used for enzyme purification. Supplementary Figures 2 and 3 show the kinetic analysis of Lf-β-glucosidase. Supplementary Table 1 shows the effect of various concentrations of ethylenediamine on β-glucosidase immobilization. Supplementary Table 2 provides detailed kinetic and inhibitory parameters for both the free and immobilized forms of the enzyme. These data demonstrate the functional properties of the immobilized biocatalyst and support its potential for repeated use in dairy bioprocessing applications. All supplementary content corresponds to data referenced in the main manuscript.