A comparison of dual-enzyme immobilization by magnetic nanoparticles and magnetic enzyme aggregates for cascade enzyme reactions.

Immobilized enzymes have been widely used for their efficiency, economy, and environment friendly. In this case, a simpler and effective immobilization method has been developed. In this study, the enzyme immobilized by magnetic beads with genipin (MGE) was prepared by mixing genipin-modified nano-Fe 3 O 4 with (R)− 1-phenylethanol dehydrogenase ((R)-PEDH) and recombinant glucose dehydrogenase (rGDH), and the magnetic cross-linked enzyme aggregates (MCLEAs) was prepared by stirring a mixture of the sulfur precipitate of the (R)-PEDH and rGDH, poly-L-lysine, and cross-linkers. When o-phthalaldehyde (o-PA) was used as a cross-linking agent for the MCLEAs preparation, a protein loading of 99.9% and 62.93% recovery activity of (R)-PEDH and 70.12% of rGDH were obtained. Compared to the MGE, the MCLEAs possessed better enzyme activity recovery. Furthermore, this study tried the synthesis of (R)− 1-(furan-2-yl) ethanol by the immobilized enzymes and obtained a concentration of 1.10 mM for the MCLEAs and 0.24 mM for the MGE at 48 h. This study explored a facile method for co-immobilization of (R)-PEDH and rGDH to synthesize (R)− 1-(furan-2-yl) ethanol. [Display omitted] • A comparison of the enzyme activity of MCLEAs and MGE. • The process of the preparation of MCLEAs using o-phthalaldehyde as the cross-linker was explored. • The MCLEAs was applied for the synthesis of (R)− 1-(furan-2-yl) ethanol. [ABSTRACT FROM AUTHOR]