Artificial Carbonic Anhydrase via the Molecular Imprinting Approach for Carbon Dioxide Bioconversion


INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH, vol.60, no.24, pp.8714-8719, 2021 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 60 Issue: 24
  • Publication Date: 2021
  • Doi Number: 10.1021/acs.iecr.1c01564
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Applied Science & Technology Source, Aqualine, Chemical Abstracts Core, Chimica, Compendex, Computer & Applied Sciences, zbMATH, DIALNET
  • Page Numbers: pp.8714-8719
  • Hacettepe University Affiliated: Yes


Carbonic anhydrase, an enzyme responsible for CO2 bioconversion in mammals, is one of the most effective CO2 hydratase catalysts in nature. Molecularly imprinted polymers have been widely utilized as a selective adsorbent and specific biorecognition element in many applications of medicine, chemistry, biology, and environmental and food sciences. If the substrate molecules are imprinted into the polymer structure to form the cavities, it is also possible to create artificial active sites for catalytic reaction. Herein, it was aimed to develop bioinspired, efficient, and environmentally friendly artificial enzymes. Under the study, CO2-imprinted hydroxyethyl methacrylate-based cryogel membranes (plastic enzymes) for CO2 bioconversion by means of the polymerizable L-histidine derivative (MAH) were synthesized and the characterization of the developed cryogel membranes was performed via scanning electron microscopy with energy-dispersive X-ray analysis, Fourier transform infrared spectroscopyattenuated total reflection, and swelling test measurements. Enzymatic activity was performed based on the electrometric method developed by Wilbur and Anderson. The Wilbur-Anderson units for the cryogel membrane containing the MAH-Zn2+ complex (1.0 mL) were calculated considering the increasing amount (from 1 to 6) of membranes to be 1.07, 1.35, 1.40, 1.63, 2.01, and 2.56.