Amphiphilic Nanointerface: Inducing the Interfacial Activation for Lipase.

Area of Science:

• Biotechnology
• Materials Science
• Biochemistry

Background:

• Graphene oxide (GO) offers tunable interfacial properties for enzyme immobilization.
• Lipase TL (Thermomyces lanuginosus) exhibits weak catalytic activity due to an inconspicuous active site lid.

Purpose of the Study:

• To design amphiphilic nanobiological interfaces between GO and lipase TL.
• To optimize the reduction degree of GO for enhanced lipase TL interfacial activation and stability.

Main Methods:

• Molecular dynamics simulations were employed to study interfacial properties.
• Facile chemical modulation was used to tune the reduction degree of GO.
• Enzyme activity assays and stability tests were conducted.

Main Results:

• Reduced graphene oxide (rGO) after 4h ascorbic acid reduction boosted lipase TL relative activity to 208%.
• This activity was 48% higher than pristine GO and 120% higher than rGO after 48h reduction.
• The modified lipase TL-GO-4h showed enhanced tolerance to heat, organic solvents, and long-term storage.

Conclusions:

• Nanomaterials with controlled hydrophilicity can facilitate lipase interfacial activation and improve enzyme stability.
• The study reveals the mechanism of enzyme activity enhancement by graphene-based nanomaterials.
• This work demonstrates the potential for extensive application of optimized nanobiological interfaces.