Comparison of Four Immobilization Methods for Different Transaminases

Biocatalytic syntheses often require unfavorable conditions, which can adversely affect enzyme stability. Consequently, improving the stability of biocatalysts is needed, and this achieved by immobilization. In study, we aimed to compare soluble immobilized transaminases from different species. A cysteine in a consensus sequence was converted single aldehyde formylglycine-generating for directed single-point attachment amine beads. This immobilization compared cross-linked aggregates (CLEAs) multipoint attachments glutaraldehyde-functionalized amine- epoxy-beads. Subsequently, reactivity (i.e., thermal, storage, solvent stability) all were analyzed under conditions. The effect highly dependent on type enzyme, strategy, application itself, with no superior technique identified. Immobilization HAGA-beads resulted highest activities up 62 U/g beads, beads best hexameric transaminase Luminiphilus syltensis. Furthermore, enabled its reusability at least 10 cycles, while maintaining full or high activity. Upscaled kinetic resolutions (partially performed SpinChemTM reactor) conversion, maintained enantioselectivity, product yields, demonstrating their applicability.