Abstract
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 β-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 β-galactose when compared to free enzyme solution, as well as enzyme immobilized on a glassy carbon electrode.
Highlights
Enzymes are excellent biological catalysts, highly specific, and fundamental in biochemical reactions
Immobilization was performed at different concentrations, while contact angle measurements and atomic force microscopy were made to verify the presence of enzymes on the paper surface
Through cross-section thickness evaluation of two different investigated graphene papers, we found 148 μm for EG paper and 23 μm for GO paper, showing higher compaction in GO paper
Summary
Enzymes are excellent biological catalysts, highly specific, and fundamental in biochemical reactions. We prepare two graphene-based papers with different hydrophilicity, GO and EG, aiming to evaluate their efficiency as a support to provide β-galactosidase enzyme immobilization aiming to improve selectivity and activity of this biocatalyst in the reaction of conversion of lactose in glucose and galactose.
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