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