Highly enhanced activity and stability via affinity induced immobilization β-glucosidase from Aspergillus niger onto...

In this study, an enzyme immobilization method for the effective biotransformation of ginsenoside Rb1 to impart activity and stability was developed. Using a hydrolase enzyme model, β-glucosidase from Aspergillus niger, immobilization within chemically affinity-linked amino-based silica provided an immobilization efficiency 5.86-fold higher than that of free enzyme. Compared with the free enzyme, the immobilized enzyme functioned optimally at a wider pH range and had higher thermostability. The optimum pH for the free and immobilized enzymes was 5.5. The optimal reaction temperature of the immobilized enzyme was 45 °C, which was 5 °C higher than that of the free enzyme. The Michaelis constant (K_m) values before and after immobilization were 0.482 mmol•L^-1 and 0.387 mmol•L^-1, respectively. The catalytic rate (K_cat) for the immobilized and free enzymes was 22.269 mmol•L^-1and 8.800 mmol•L^-1, respectively, and the catalytic efficiency (K_cat/K_m) activity of the immobilized enzyme was 3.30-fold higher than that of the free enzyme. The immobilized enzyme could preserve 97 % of the activity after 45 cycles of repeated use. The high catalytic activity and significant operational stability are beneficial for industrial applications.