A facile immobilization of polyphenol oxidase enzyme on graphene oxide and reduced graphene oxide thin films: An insight into in-vitro activity measurements and characterization

摘要: Abstract Graphene oxide (GO) and reduced graphene (rGO) Langmuir-Blodgett (LB) films with specific surface properties functional groups were prepared as negative ideal substrates. Immobilization of the polyphenol oxidase (PPO) enzyme on these was easily accomplished by electrostatic interaction without need for any chemical bonding or modification. The PPO binding regions to GO rGO surfaces shown an potential map pH: 5.0 value. catalytic performances immobilized substrates found be higher in GO-PPO LB compared RGO-PPO in-vitro media. reason why activity is than rGO-PPO also proved SEM studies. immobilization onto both thin complexes further demonstrated FT-IR measurement. This study revealed that biodegradable superior inorganic materials terms its use biological systems. In addition, fact regular film structures a single molecule thickness technique, contributed stability recycling rGO. this respect, storage determined one month at +4 °C.