Metal oxide–based macroporous ordered double affinity molecularly imprinted polymer for specific separation and enrichment of glycoprotein from food samples: a co-modification of DMSA and boronate affinity

Metal oxide–based macroporous ordered double affinity molecularly imprinted polymers (D-MIPs) were developed as solid phase extraction (SPE) adsorbents for the specific identification of ovalbumin (OVA) under physiological pH conditions prior to ultraviolet visible (UV–vis) spectrophotometric detect...

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Published in:Mikrochimica acta (1966) Vol. 189; no. 1; p. 43
Main Authors: Guo, Bailin, Tong, Yukui, Sun, Baodong, Zhang, Baoyue, Chen, Xue, Bi, Sheng, Tian, Miaomiao
Format: Journal Article
Language:English
Published: Vienna Springer Vienna 01-01-2022
Springer
Springer Nature B.V
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Summary:Metal oxide–based macroporous ordered double affinity molecularly imprinted polymers (D-MIPs) were developed as solid phase extraction (SPE) adsorbents for the specific identification of ovalbumin (OVA) under physiological pH conditions prior to ultraviolet visible (UV–vis) spectrophotometric detection. Herein, macroporous alumina (MA) was used as a matrix; dimercaptosuccinic acid (DMSA) and 3-aminophenylboric acid (APBA) were employed as dual-functional monomers; APBA is a self-polymerizing monomer. The effects of synthesis conditions, SPE conditions as well as selectivity, reproducibility, and reusability were studied. The co-modification of DMSA and boronate affinity renders the adsorbent exhibiting a high adsorption capacity (114.4 mg g −1 ) and short equilibrium time (30 min). The surface imprinting technology causes the adsorbent to have high selectivity towards OVA. The OVA recovery range is 91.1–99.6%. This study provides a promising method for the enrichment of OVA and other cis-diol-containing analytes in complex biological samples. Graphical abstract A novel metal oxide–based macroporous ordered nanoparticle with a combination of DMSA and boronate affinity was successfully prepared for specific separation and enrichment of glycoprotein from complex biological samples.
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ISSN:0026-3672
1436-5073
DOI:10.1007/s00604-021-05155-8