## 1 Introduction  
Chlorophenols, a class of important chemicals that are used in the industrial field, can cause serious pollution due to their aromatic structure and high toxicity [1; 2]. Therefore, the degradation of chlorophenol pollution is urgent and has attracted extensive attention. Although a variety of physical, chemical, and biological methods have been used towards this end, most of these have certain limitations, such as high energy consumption, high costs, and low degradation efficiency [3; 4; 5], limiting their large-scale application. In recent years, biodegradation has emerged as one of the most promising technologies for treating harmful organic pollutants from the viewpoints of sustainable chemistry and green chemistry, due to its higher environmental friendliness, higher selectivity, and more efficient mineralization compared with other methods [6]. Further, the potential for biodegradation to be used to remove chlorophenols in water has attracted considerable research attention. Lacases (EC 1.10.3.2), found in fungi, plants, bacteria, and insects, belong to the blue-copper enzyme family. They have broad substrate specificity and eco-friendliness [7]. Inaddition, lacases can catalyze the one-electron oxidation of various organic and inorganic substrates, including phenols, ketones, phosphates, ascorbate, amines, and lignin. Free lacases extracted from nature have the disadvantages of poor stability, a short lifespan, being difficult to recycle, and high cost, meaning it is generally difficult for them to tolerate harsh industrial processing conditions [8; 9; 10]. Researchers have mainly modified enzymes through protein engineering, non-covalent modification, chemical modification, and immobilization [11; 12; 13]. However, in practice, protein engineering still faces many challenges. After protein modification, lacases exhibit unstable properties with regard to their preservation and application [14]. Both the covalent modification and non-covalent modification of enzyme systems are unstable, and the activity and stability of enzymes may be reduced after modification. Therefore, enzyme immobilization technology is ideal for compensating for the deficiency of free enzymes [15; 16]. One of the significant advantages of enzyme immobilization is that it provides an expected ideal enzyme system that can be reused for a couple of cycles, reducing operation costs [11; 17]. Currently, enzyme immobilization strategies mainly focus on supports innovation through the use of metallic compounds [18], carbon-based materials [19], silicon-based nanomaterials [20], metal-organic frameworks or their derivatives [14], polymers [21], etc. [PERSON] and co-workers immobilized increase into carbon-based mesoporous magnetic composites through adsorption. The system was able to retain above 70% of its initial activity after five cycles [22]. [PERSON] and colleagues encapsulated lacase in MOF and realized high activity of lacase under high-temperature conditions [23]. [PERSON] and colleagues developed a method of lacase immobilization based on nanofibrous membranes consisting of electrospun chitosan/poly (vinyl alcohol) composites. Compared with free lacase, the combined removal of 2,4-DCP was significantly improved by the immobilized lacase [21]. However, there are still some challenges that need to be resolved prior to enzyme immobilization's industrial application, such as enzyme leakage, toxicity, the low surface area involved, and the supports' high cost. Therefore, it is highly desirable to develop novel supports to achieve the effects of the high load, low leakage, high activity, and high stability of enzymes. In the past few decades, the application of polymeric ionic liquid (PIL)-based biomaterials has attracted wide attention. PILs are one type of conductive polymer that have an IL structure in the repeating unit, where the anions or cations of the PILs are confined in the matrix of the macromolecules.