Immobilization of snailase and β-glucosidase on L-aspartic acid-modified magnetic amorphous ZIF for efficiently and sustainably producing ginsenoside compound K.

Improving the catalytic efficiency and recyclability of immobilized enzyme remained a serious challenge in industrial applications. Enzyme immobilization in the amorphous zeolite imidazolate framework (aZIF) preserved high enzyme activity, but still faced separation difficulties and a low catalytic efficiency in practice. In this study, a one-pot co-precipitation method was used to form the enzyme-aZIF/magnetic nanoparticle (MNP) biocomposite by rapidly precipitating snailase (Sna) and β-glucosidase (β-G) with metal/ligand on MNP and modifying with L-aspartic acid (Asp). Thanks to Asp modification protecting the natural conformation of internal protein molecules and MNP stabilizing the conformation of active enzymes after immobilizing, Sna&β-G in the carrier had more stable conformations and higher catalytic efficiency than those in conventional ZIF-8, increasing the catalytic efficiency for converting ginsenoside Rb1 to rare ginsenoside compound K (CK) to 79.16 %. Moreover, while improving the stability of Sna&β-G, owing to the magnetism imparted by MNP, the immobilized enzyme maintained high enzyme activity and recovery after 7 cycles by rapid magnetic separation. The results provided guidance for developing immobilized Sna&β-G biocomposites with ideal catalytic efficiency and easy recovery to catalyze ginsenoside Rb1 to rare ginsenoside CK.