Enzyme-catalyzed cascade reactions on multienzyme proteinosomes

In this research, to mimic the structures and the functionalities of the organelles in living cells multienzyme proteinosomes with p-galactosidase (p-gal), glucose oxidase (GOx) and horseradish peroxidase (HRP) on the surfaces are fabricated by hydrophobic-interaction induced self-assembly approach. To investigate the mechanism of the formation of proteinosomes, poly(di(ethylene glycol) methyl ether methacrylate) (PDEGMA) and bovine serum albumin are employed in a model system and the study demonstrates that the hydrophobic interaction between the dehydrated polymer chains and the hydrophobic patches on the proteins plays a key role in the fabrication of the proteinosomes. Based on the model system, multienzyme proteinosomes with p-gal, GOx and HRP on the surfaces are fabricated through hydrophobic interaction between PDEGMA and enzyme molecules. Enzyme catalyzed cascade reactions are performed on the surfaces of the proteinosomes, and the immobilized enzymes show higher bioactivities than the free enzymes, due to the direct transfer of the product as a substrate from one enzyme molecule to another. This research provides a unique method for the synthesis of multienzyme proteinosomes with improved bioactivities, and the biofunctional structures will find promising applications in medical and biological science. (c) 2021 Elsevier Inc. All rights reserved.

Automated summary

By utilizing hydrophobic interaction, multienzyme proteinosomes are fabricated with p-gal, GOx, and HRP on the surfaces in a model system using PDEGMA and bovine serum albumin. The immobilized enzymes show higher bioactivities than the free enzymes, facilitating direct transfer of the product as a substrate from one enzyme molecule to another.