Convenient Immobilization of α‐L‐Rhamnosidase on Cerium‐based Metal‐Organic Frameworks Nanoparticles for Enhanced Enzymatic Activity and Recyclability. Issue 3 (20th December 2021)

• Record Type: Journal Article
• Authors: Peng, Lingling; Tan, Wansen; Lu, Yuting; Yao, Ayan; Zheng, Dayuan; Li, Le; Xiao, Jingran; Li, Lijun; Li, Qingbiao; Zhou, Shu‐feng; Zhan, Guowu
• Is Part Of: ChemCatChem. Volume 14:Issue 3(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-12-20
• Subjects: α-L-Rhamnosidase -- enzyme immobilization -- membrane reactor -- metal-organic framework -- reusability; Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.202101489
• Languages: English
• ISSNs: 1867-3880

Abstract

Abstract: The α‐L‐Rhamnosidase (Rha) is a useful glycoside hydrolase for selectively hydrolyzing the terminal L‐rhamnose residues in flavonoids, being vital to food and pharmaceutical industries. However, Rha suffers from low recyclability and poor stability in harsh environments. Herein, we explored five typical metal‐organic frameworks (MOFs) as porous carriers to immobilize Rha, and the activities of the resultant Rha@MOF composites were compared with the free enzyme. The locations of the enzyme in MOFs were proved by a series of characterization techniques. It was found that Rha@Ce‐BTC (with enzyme immobilization efficiency of 23 % and enzyme loading content of 8.8 %) showed the highest enzymatic activity. The immobilized Rha@Ce‐BTC showed 80 % residual activity after five consecutive cycles, suggesting a limited leaching effect. Also, Rha@Ce‐BTC manifested markedly enhanced enzyme‐substrate affinity and catalytic efficiency compared to free Rha, as supported by Michaelis‐Menten kinetic studies. Accordingly, the Ce‐BTC would be an appealing carrier for enzyme immobilization, and the as‐designed enzyme/Ce‐BTC composites are promising candidates for industrial use with remarkably high activity, recyclability, and storage stability. Abstract : Immobilized Rha on MOFs : Herein, we explored five typical metal‐organic frameworks (MOFs) as porous carriers to immobilize Rha, and the obtained Rha@Ce‐BTC showed the highest enzymatic activity. Also, Rha@Ce‐BTC manifested enhanced enzyme‐substrate affinity, great reusability/storage stability, and catalytic efficiency compared to free Rha. Significantly, the as‐prepared Rha@Ce‐BTC might be assembled as a membrane reactor for efficient biocatalysis reactions.