Convenient Immobilization of α‐L‐Rhamnosidase on Cerium‐based Metal‐Organic Frameworks Nanoparticles for Enhanced Enzymatic Activity and Recyclability

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.

Construction of Immobilized Enzymes with Yeast and Metal–Organic Frameworks for Enhanced Biocatalytic Activities

“…Furthermore, substrate concentration for the enzymatic reaction is crucial for the catalytic efficiency, which can be expressed by K M (Michaelis–Menten constant) value, and the K M value plays a key role in assessing the affinity between the enzyme and the substrate. , The enzymatic kinetics of Y@ZIF-8@t-CAT and free catalase were monitored using different concentrations of substrates (Figure S13), and the reaction kinetic parameters for Y@ZIF-8@t-CAT and free catalase are shown in Table S6. Generally, a higher K M value corresponds to a lower affinity toward the substrate.…”

Enzyme Kinetic of Lipase Catalysed Acidolysis of Used Cooking Palm Oil

“…Table 2 summaries the values of Km and Vmax in various units. The combination of a low Km value and a high Vmax value is the most favourable, indicating a high enzymesubstrate affinity (Peng et al, 2022). Km and Vmax values of lipases vary greatly (Kuo et al, 2020).…”