Bio-inspired multifunctional and reusable LiP@MFO-GO and LiP@MFO-Chit hybrid enzyme complexes for efficient degradation of melanin.

Melanin is a complex brown pigment, primarily responsible for the skin pigmentation. Therefore, cosmetic industries have always been in search of potent oxidative enzymes useful for melanin degradation, and to promise a fair complexion after using their products. In the present study, lignin peroxidase from Pseudomonas fluorescence LiP-RL5 isolate has been immobilized on super-paramagnetic nanoparticles to enhance its stability and reusability.

Fabrication of thermostable and reusable nanobiocatalyst for dye decolourization by immobilization of lignin peroxidase on graphene oxide functionalized MnFeO superparamagnetic nanoparticles.

In view of the potential applications of immobilized enzymes, partially purified Lignin Peroxidase (LiP) from Pseudomonas fluorescens LiP-RL5 was immobilized on Graphene Oxide functionalized MnFeO nanoparticles (10 nm, synthesized by sol-gel auto-combustion) to fabricate a new hyperactive and thermostable nanobiocatalyst and thereafter characterized by using standard techniques. Immobilized LiP was quite stable at 50 °C with the half-life of 14 h and showed higher tolerance towards various metal ions and solvents than free LiP. Immobilized LiP retained 50% of enzyme activity even after nine consecutive runs.