Techniques for immobilizing enzymes to create durable and effective biocatalysts

Abstract

This comprehensive review focuses on strategies for creating efficient and robust immobilized biocatalysts. It explores various physicochemical approaches that hold promise for enzyme stabilization and enhancement of catalytic potential. One approach involves designing enzyme stabilization on permeable scaffolds, emphasizing the importance of the support structure and the ability to fine-tune biocatalyst activity. Another pathway is establishing covalent bonds between enzymes and support surfaces, anchoring the biocatalysts for longevity and sustained activity in industrial and research applications. Polymers are also used to modify the structure and formulation of immobilized enzymes, enhancing stability and providing a versatile platform for biocatalytic reactions. These approaches are particularly valuable when enzymes are immobilized within pre-established permeable scaffolds. They enable researchers and engineers to utilize biocatalysis in diverse applications, such as biopharmaceutical production and sustainable chemical synthesis. Furthermore, these fixed-stabilized enzyme derivatives offer significant advancements in enzyme reaction optimization and reactor design. The reported enhancements in catalytic activity are remarkable, with performance gains ranging from 500 to an impressive 20,000-fold compared to diluted soluble enzymes. In summary, this review highlights the importance of innovative strategies for developing immobilized biocatalysts. It presents exciting avenues for researchers and industries seeking to harness the catalytic potential of enzymes in various applications. These advancements not only promise enhanced efficiency but also contribute to sustainable and environmentally friendly chemical processes.

Keywords

• Immobilized biocatalysts
• Enzyme stabilization
• Reactor design
• Chemical connections
• Biocatalytic reactions
• Hydrogen permeability