Laccase (E.C.1.10.3.2) is a series of multi-copper oxidases which utilizes molecular oxygen as an electron acceptor and is capable of catalyzing the simultaneous reduction of a wide range of phenolic compounds and aromatic amines to water with its co-substrate oxygen [
4,
5]. Laccase has been widely used in the fields of biofuel cells, biosensors, bioremediation, and wastewater treatment due to its excellent substrate specificity [
6,
7]. However, its low operational stability and difficulties in separation and reuse limit its practical use. How to effectively improve stability and reusability and maintain the activity of laccase has become a hot topic of research [
8]. Immobilization technology is a fundamental means of achieving enzyme cost targets and realizing the advantages of enzyme technology. The immobilized enzyme can be easily separated from the product, simplifying the post-treatment process and facilitating the recovery and reuse of the enzyme [
9]. The thermal stability, organic solvent tolerance, and storage stability may be further enhanced after immobilization, which is conducive to improving its value in practical applications [
10]. Currently, nanocarriers have been widely used in the field of immobilized enzymes because of their large specific surface areas, low mass transfer limits, easy recovery, and good stability [
11,
12]. Among nanomaterials, nanosilica (SiO
2) is widely used in nanoindustries, biotechnology, biomedical and pharmaceutical fields due to its low price, non-toxicity, large specific surface area, and additional advantages [
13–
15]. However, immobilizing enzymes directly on silica normally result in low catalytic performance due to the inherently inert surface properties of silica [
16]. The surface modification of inorganic materials generally requires refluxing in organic solvents, which is not only time-consuming and laborious but also conducive to toxic solvents to remain in the pores of the material. This cumbersome process limits a wide range of practical applications [
17]. Therefore, it is necessary to find a simple and environmentally friendly method to modify inorganic materials to prepare feasible carriers for the immobilization of enzymes. The dopamine molecule, containing catechol and an amino group, can form coatings on a variety of different substrates under weakly alkaline conditions, and these coatings can be easily functionalized and have a good application prospect [
18]. The immobilization process is fast and easy with direct contact between the enzyme and the carrier. However, the enzyme usually loses its three-dimensional structure, and its activity could be decreased [
19–
21].