Immobilization and characterization of β-galactosidase from Aspergillus oryzae in PVA-CMC hydrogel.

Creating new formulations of immobilized enzymes has been a major focus of modern biotechnology. In this study, the industrially significant β-galactosidase was immobilized by being trapped in a polyvinyl alcohol and carboxymethyl cellulose (PVA-CMC) gel. The immobilized enzyme was optimized and characterized, and the results were compared with those obtained using free enzymes. The data show that 40 °C to 50 °C is the ideal temperature range for the enzyme after immobilization. The activity rose, the Vmax value increased from 1.94 U/mg to 6.01 U/mg, and the Km value fell from 4.86 mM to 3.35 mM at pH 5, the optimal pH. β-galactosidases immobilized on PVA-CMC gels exhibited 70 % activity at the end of the fifth week and 50 % activity at the end of the eighth week, depending on the storage stability of the immobilized enzyme. After three reuses, the initial activity of the enzymes decreased, yet the thermal stability of the immobilized enzyme remained superior to that of the free form, retaining 82 % of its initial activity. Thus, it might be claimed that immobilization amplifies the enzyme's catalytic impact. Consequently, it has been discovered that immobilized β-galactosidase exhibits stronger enzymatic characteristics than free β-galactosidase, making it potentially more useful in industrial operations.