Tailoring surface properties of functionalized graphene papers aiming to enzyme immobilization

The use of enzymes as catalysts requires recovery and reuse to make the process viable. Enzymatic immobilization changes enzyme stability, activity, and specificity. It is very important to explore new substrates for immobilization with appropriate composition and structure to improve the efficiency of the immobilized enzymes. This work explores the use of two different graphene oxide papers, one produced by oxidation route (GO) and the other by electrochemical synthesis (EG), aiming for beta-galactosidase immobilization. The chemical and structural properties of these two papers were characterized by Raman spectroscopy, X-ray photoelectron spectroscopy and X-ray diffraction. Atomic force microscopy images showed that EG paper ensured more efficient immobilization of the enzymes on the surface of the paper. Cyclic voltammetry was used to monitor the reaction of conversion of lactose to glucose in the free enzyme solution and graphene paper immobilized enzyme solutions. The cyclic voltammetry analysis showed that immobilized enzymes on GO paper showed an improvement in the activity of beta-galactose when compared to free enzyme solution, as well as enzyme immobilized on a glassy carbon electrode.

Automated summary

In the study of enzyme immobilization, two different graphene oxide papers were used to immobilize beta-galactosidase, with electrochemical synthesis (EG) paper showing more efficient enzyme immobilization. Cyclic voltammetry analysis indicated that enzymes immobilized on GO paper exhibited improved beta-galactose activity compared to free enzyme solution and enzyme immobilized on a glassy carbon electrode.