Figure 6 The adsorption kinetics of BSA on MTCFs@SIP@CBMA and MTCFs@NIP@CBMA. Error bars represent ± standard deviations, n = 3.
3.4.2 Adsorption thermodynamics
The adsorption capacities of MTCFs@SIP@CBMA and MTCFs@NIP@CBMA varied with the initial concentration of BSA as shown in Figure 7. For MTCFs@SIP@CBMA, when the concentration of BSA was lower than 0.1 mg/mL, the adsorption capacity gradually increased with the increase of concentration. When the concentration reached 0.1mg/mL, the adsorption capacity tended to be stable. This was an indication that the adsorption capacity of MTCFs@SIP@CBMA on BSA achieved saturation at this moment. The equilibrium adsorption capacity was 392.75 mg/g, which was significantly higher than that of MTCFs@NIP@CBMA at 57.96 mg/g. Consequently, the calculated imprinting factor was 6.78. The outcomes illustrated that the recombination of BSA on MTCFs@SIP@CBMA occurred based on the imprinting sites. Otherwise, the imprinting effect was significantly improved due to the introduction of anti-protein adsorption chain CBMA, which reduced the non-specific adsorption. Compared with the reported adsorption properties and IF values of imprinted materials (see Table 2), MTCFs@SIP@CBMA exhibited fast adsorption rate, high adsorption capacity and considerable IF values, which could achieve efficient protein separation in solution.
Figure 7 Adsorption isotherms of MTCFs@SIP@CBMA and MTCFs@NIP@CBMA for BSA. Error bars represent ± standard deviations, n = 3.
Table 2 Comparison of QMIP, adsorption equilibrium time and IF for reported imprinted materials