A rational approach for 3D recognition and removal of L-asparagine via molecularly imprinted membranes
In this study, a L-asparagine (L-Asn) imprinted membranes (L-Asn-MIPs) were synthesized via molecular imprinting for selective and efficient removal of L-Asn. The L-Asn-MIP membrane was prepared by using acrylamide (AAm) and hydroxyethyl methacrylate (HEMA) as a functional monomer and a comonomer, r...
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Veröffentlicht in: | Journal of pharmaceutical and biomedical analysis 2023-03, Vol.226, p.115250-115250, Article 115250 |
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Sprache: | eng |
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Zusammenfassung: | In this study, a L-asparagine (L-Asn) imprinted membranes (L-Asn-MIPs) were synthesized via molecular imprinting for selective and efficient removal of L-Asn. The L-Asn-MIP membrane was prepared by using acrylamide (AAm) and hydroxyethyl methacrylate (HEMA) as a functional monomer and a comonomer, respectively. The membrane was characterized by scanning electron microscopy (SEM) and Fourier Transform infrared spectroscopy (FTIR). The L-Asn adsorption capacity of the membrane was investigated in detail. The maximum L-Asn adsorption capacity was determined as 408.2 mg/g at pH: 7.2, 24 °C. Determination of L-Asn binding behaviors of L-Asn-MIPs also shown with Scatchard analyses. The effect of pH on L-Asn adsorption onto the membrane and also the selectivity and reusability of the L-Asn-MIPs for L-Asn adsorption were determined through L-asparaginase (L-ASNase) enzyme activity measurements. The selectivity of the membrane was investigated by using two different ternary mixtures; L-glycine (L-Gly)/L-histidine (L-His)/L-Asn and L-tyrosin (L-Tyr)/L-cystein(L-Cys)/L-Asn. The obtained results showed that the L-Asn-MIP membranes have a high selectivity towards L-Asn.
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•L-asparagine imprinted membranes were synthesized for efficient removal of L-Asn.•The membranes were characterized by FT-IR and SEM.•The specificity of the membranes was also confirmed by enzyme activities.•L-Asn-IPs membranes have high selectivity towards L-Asn. |
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ISSN: | 0731-7085 1873-264X |
DOI: | 10.1016/j.jpba.2023.115250 |