Amphiphilic Nanointerface: Inducing the Interfacial Activation for Lipase

Abstract

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.

Single-Crystalline Ordered Nanoporous Metal–Organic Frameworks for Lipase Immobilization and Structured Lipid Production

“…54 The diminished accessibility of lipase, resulting from the weak wettability of the hydrophobic carrier, is considered the primary reason for the declined loading efficiency of SOM-MIXs. 55 The decreased external surface area as described previously led to a further decreasing loading efficiency with the increase of the 1,2,3-benzotriazole ratio. Moreover, the higher specific activity and activity recovery observed in the SOM-MIXs can be ascribed to the interfacial activation of lipase on the hydrophobic carrier.…”

Covalent immobilization of lipase on an ionic liquid-functionalized magnetic Cu-based metal–organic framework with boosted catalytic performance in flavor ester synthesis

“…When lipase was placed at a hydrophobic interface, interface activation occurred which opens the lid and made the active center accessible. 36 Herein, we use the water contact angle (WCA) to assess the hydrophobicity of supports and the WCA images of samples are shown in Fig. 4.…”

Energetic and Kinetic Origins of CALB Interfacial Activation Revealed by PaCS-MD/MSM

“…The interfacial activation of lipases was observed for different types of hydrophobic surfaces, e.g., the substrate , and solid surfaces. , An early study showed that CALB does not exhibit significant interfacial activation compared to other lipases . However, a later report indicated the interfacial activation of CALB immobilized on a highly hydrophobic surface toward a bulky substrate .…”