Agarose vs. Methacrylate as Material Supports for Enzyme Immobilization and Continuous Processing

Enzyme immobilization has become a key strategy to improve the stability and recycling of biocatalysts, resulting in greener and more cost-efficient processes. The design of the immobilized catalysts is often focused only on the immobilization strategy, the binding chemistry between the enzyme and the support, while less attention has been paid to the physico-chemical properties of material supports. Selecting the best carrier for a specific application may greatly influence the performance of the biocatalytic reaction. Herein, we present a comparative study between the two most used material supports for protein immobilization, agarose and methacrylate. Hydrophilic agarose microbeads ensure higher retained enzymatic activity and better catalyst performance when hydrophobic compounds are involved in the biotransformation. Due to the high stickiness, lipophilic molecules represent a major limitation for methacrylate carriers. O-2-dependent reactions, in contrast, must be carried out by immobilized enzymes on methacrylate supports due to the low mechanical stability of agarose under dehydration conditions. All these parameters were tested with a special focus on continuous-flow applications.

Automated summary

The study found that hydrophilic agarose microbeads exhibit higher retained enzymatic activity and better catalyst performance, especially for biotransformation involving hydrophobic compounds. In contrast, lipophilic molecules pose a major limitation for methacrylate carriers, and O-2-dependent reactions must be carried out by immobilized enzymes on methacrylate supports due to the low mechanical stability of agarose under dehydration conditions.