Amphiphilic Nanointerface: Inducing the Interfacial Activation for Lipase

Graphene-based materials are widely used in the field of immobilized enzymes due to their easily tunable interfacial properties. We designed amphiphilic nanobiological interfaces between graphene oxide (GO) and lipase TL (Thermomyces lanuginosus) with tunable reduction degrees through molecular dynamics simulations and a facile chemical modulation, thus revealing the optimal interface for the interfacial activation of lipase TL and addressing the weakness of lipase TL, which exhibits weak catalytic activity due to an inconspicuous active site lid. It was demonstrated that the reduced graphene oxide (rGO) after 4 h of ascorbic acid reduction could boost the relative enzyme activity of lipase TL to reach 208%, which was 48% higher than the pristine GO and 120% higher than the rGO after 48 h of reduction. Moreover, TL-GO-4 h's tolerance against heat, organic solvent, and long-term storage environment was higher than that of free TL. The drawbacks of strong hydrophobic nanomaterials on lipase production were explored in depth with the help of molecular dynamics simulations, which explained the mechanism of enzyme activity enhancement. We demonstrated that nanomaterials with certain hydrophilicity could facilitate the lipase to undergo interfacial activation and improve its stability and protein loading rate, displaying the potential of the extensive application.

Automated summary

This study investigates the use of graphene-based materials as immobilized enzymes in the field of biocatalysis. The researchers designed a nanobiological interface between graphene oxide (GO) and lipase TL, which could be tuned through molecular dynamics simulations and chemical modulation. The reduced graphene oxide (rGO) showed improved catalytic activity compared to GO, and 4 hours of reduction with ascorbic acid yielded the highest enzyme activity. The study also explored the drawbacks of hydrophobic nanomaterials on enzyme production and suggested the potential of hydrophilic nanomaterials in enhancing enzyme activity.