Editorial: Designing Carrier-Free Immobilized Enzymes for Biocatalysis
Susana Velasco‐Lozano, Javier Rocha‐Martín, José Cleiton Sousa dos Santos
Abstract
Global challenges in energy, resources, environment and sustainable chemical processing are leading us to minimize the use of natural resources, toxic materials, energy, and the generation of waste and pollutants. Enzymatic biocatalysis development evolves to strengthen the ongoing required process improvements of current industrial chemical transformations, where enzymes are naturally available, efficient biocatalysts exhibiting high specificity and enantioselectivity. However, for their industrial application, enzymes must possess high stability under large-scale producing conditions (such as high substrate and product concentrations, temperature, presence of solvents), where enzymes easily become inactive due to their low stability under such unnatural conditions or the almost null activity toward non-natural substrates. In this context, enzyme immobilization is a strategy that can facilitate their stabilization, purification, and reuse in the industry Enzymes can be immobilized on water-insoluble supports or without supports. Among carrier-free immobilization methods, the Cross-Linked Enzyme Aggregates (CLEA) emerged as a promising technology capable of manufacturing robust immobilized protein aggregates. In general, the preparation of CLEA involves the first stage of precipitation of enzymatic molecules followed by a cross-linking step managed by the action of a bifunctional reagent added to the reaction system, the cross-linker. As a result, the aggregates become insoluble, maintaining high catalytic activity, excellent stability, and low production cost.