Co-immobilized β-glucosidase and snailase in green synthesized Zn-BTC for ginsenoside CK biocatalysis

Enzyme immobilization via metal–organic frameworks is a key step to improve the stability and catalytic activity of the enzyme for realizing the enzymatic conversion of ginsenoside compound K (CK) in industrial application. Even though current studies mainly focused on improving the stability and reusability of enzymes through immobilization, the problem of long enzyme conversion cycle has not been solved. In this study, green synthesis of Zn-BTC co-immobilized snailase (SN) and β-glucosidase (β-G) was applied to design and construct β-G&[email protected] (β-Glycosidase and snailase were co-immobilized on Zn-BTC) biocomposite. Results showed the β-G&[email protected] materials have good stability and recyclability under extreme conditions (pH, temperature, and organic solvents). At pH 8, free β-G&SN was completely inactivated, whereas β-G&[email protected] maintained 51.2% of the enzymatic activity. The conversion rate of CK with β-G&[email protected] biocomposite was 1.73 times that of immobilization of single SN, indicating significant advantages over single enzyme immobilization in terms of transformation efficiency. This work provides a green, simple, low-cost, and sustainable strategy and lays the foundation for the industrial production of ginsenoside CK through innovative design.