Magnetic Cross-Linked Enzyme Aggregates of Glycoside Hydrolase: An Efficient and Stable Biocatalyst for Icaritin

Abstract

With the booming development of natural anticancer agents, icaritin has been widely used in clinical liver cancer treatment due to the smaller number of side effects. Among them, enzymes as catalysts for producing icaritin have attracted considerable attention. Industrial production remains in its infancy due to the poor reusability of free enzymes, despite enzymes possessing favorable efficiency and green catalytic effects. The present study investigated two immobilization methods, including cross-linked enzyme aggregates (CLEAs) and magnetic cross-linked enzyme aggregates (MCLEAs). The optimal temperature and pH for the two hydrolases were determined, followed by characterization using VSM, XRD, FT-IR, and TEM techniques. The experiments have demonstrated that MCLEAs eradicate the need for ultrafiltration; MCLEAs are beneficial for enhancing fixation efficiency. Additionally, MCLEAs exhibited significantly higher catalytic activity, which raised the catalytic activity by approximately 30% compared with CLEAs. Moreover, after 10 consecutive reuse cycles, the catalytic activity of MCLEAs remained above 70%, maintaining a conversion rate of epimedin C at 61.59%. To summarize, MCLEAs offer an efficient strategy for enzyme immobilization. MCLEAs not only significantly enhanced both the enzyme’s ability to catalyze and resist but also eliminated the necessity for ultrafiltration as well as enabled rapid product separation.