Engineered tyrosinases with broadened bio-catalysis scope: immobilization using nanocarriers and applications.

Abstract

Enzyme immobilization is a widely used technology for creating more stable, active, and reusable biocatalysts. The immobilization process also improves the enzyme's operating efficiency in industrial applications. Various support matrices have been designed and developed to enhance the biocatalytic efficiency of immobilized enzymes. Given their unique physicochemical attributes, including substantial surface area, rigidity, semi-conductivity, high enzyme loading, hyper catalytic activity, and size-assisted optical properties, nanomaterials have emerged as fascinating matrices for enzyme immobilization. Tyrosinase is a copper-containing monooxygenase that catalyzes the o-hydroxylation of monophenols to catechols and o-quinones. This enzyme possesses a wide range of uses in the medical, biotechnological, and food sectors. This article summarizes an array of nanostructured materials as carrier matrices for tyrosinase immobilization. Following a detailed background overview, various nanomaterials, as immobilization support matrices, including carbon nanotubes (CNTs), carbon dots (CDs), carbon black (CB), nanofibers, Graphene nanocomposite, platinum nanoparticles, nano-sized magnetic particles, lignin nanoparticles, layered double hydroxide (LDH) nanomaterials, gold nanoparticles (AuNPs), and zinc oxide nanoparticles have been discussed. Next, applied perspectives have been spotlights with particular reference to environmental pollutant sensing, phenolic compounds detection, pharmaceutical, and food industry (e.g., cereal processing, dairy processing, and meat processing), along with other miscellaneous applications.