Marigold-like tyrosinase-embedded nanostructures—a nano-in-micro system

Abstract

Marigold-like tyrosinase-entrenched nanostructures were developed by a facile method using a metal cofactor to overcome the limitations of conventional enzyme immobilization techniques. The protein–copper complex promotes the hierarchical self-assembly of nanopetals into marigold-like microstructures through a sequential germination process. Nanopetals, which originated from bead-like tiny projections, showed budding over the surface and promoted the anisotropic growth of copper phosphate nanocrystals upon co-ordination with the active functional groups in protein. This organic–inorganic hybrid showed excellent re-usability, comparable catalytic efficiency, faster reaction rate, improved storage, and thermal stability without affecting the enzyme activity.