Fibrous all-solid-state flexible supercapacitors have attracted much attention in the functional field of wearable electronic devices due to their excellent deformability. It is very important to select suitable flexible substrate, active substance, and binding means to improve electrode performance. In this paper, carbon fiber with high conductivity and the active site was used as a flexible substrate, and FeOOH with high specific capacity was grown on the surface of carbon fiber yarn by one-step in situ electrodeposition. The influence of different deposition conditions on the morphology of FeOOH and the electrochemical performance of the flexible electrode was studied. The electrode obtained by deposition at a constant voltage of 2.5 V for 150 min has a high specific capacitance of 10.44 F cm −3 . In addition, the device has a high voltage window of 1.6 V and excellent cycle stability of 7000 cycles when formed as an all-solid-state symmetric supercapacitor.
The removal of dye pollutants from water bodies is a significant global issue due to their negative effects on both ecosystems and human health. For this purpose, effective and selective α-FeOOH-Fe3O4@Chitosan-LDHs@Lipase (MF@CS-LDHs@LIP) magnetically bionanomaterials were synthesized via co-precipitation and cross-linking methods for uptake of Congo red (CR) from wastewater. Comprehensive characterization of both the carrier and MF@CS-LDHs@LIP was performed using SEM, FTIR, XRD, BET, VSM, and EDX. The analytical results confirmed the successful immobilization of lipase on the composite carrier. The immobilization conditions and enzymatic properties of the enzyme were investigated. The results demonstrated that the immobilized lipase maintained over 60% relative activity within a pH range of 7.0–11.0. Notably, at pH 11.0, its activity was 1.69 times higher than that of free lipase. Both immobilized and free lipase exhibited significant activity reduction at temperatures exceeding 40 °C. At 55 °C, the immobilized lipase exhibited 2.32 times higher relative activity compared to its free counterpart. However, after five reuse cycles, the immobilized lipase retained 40.30% of its initial activity. Furthermore, after being stored at 4 °C for 30 days, the relative activity of immobilized lipase was slightly higher than that of free lipase, approximately 24.32% and 14.81%, respectively. The adsorption kinetics and isotherm studies revealed that the adsorption process followed pseudo-first-order kinetic and the Temkin isotherm model. A maximum adsorption capacity of 87.82 mg/g was present in CR solution at 25 °C, pH = 6.0, 420 min, 50 mg dosage, and 100 mL of an initial concentration of 120 mg/L. Furthermore, the immobilized lipase exhibited excellent reusability, maintaining a CR removal efficiency above 70% after 5 consecutive cycles.
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