Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site
| Autor: | Evgenia Korzhikova-Vlakh, Olga Solomakha, Tatiana B. Tennikova, Mariia Stepanova, Daria Ten |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Immobilized enzyme
02 engineering and technology lcsh:Chemical technology 01 natural sciences Catalysis lcsh:Chemistry Hydrolysis flow-through catalysis lcsh:TP1-1185 Physical and Theoretical Chemistry Monolith catalyzed hydrolysis chemistry.chemical_classification geography geography.geographical_feature_category Chymotrypsin biology 010401 analytical chemistry Substrate (chemistry) Polymer enzyme mimics 021001 nanoscience & nanotechnology 0104 chemical sciences lcsh:QD1-999 Chemical engineering chemistry biology.protein molecular imprinting artificial catalytic centers 0210 nano-technology Molecular imprinting macroporous polymer monoliths |
| Zdroj: | Catalysts Volume 10 Issue 12 Catalysts, Vol 10, Iss 1395, p 1395 (2020) |
| ISSN: | 2073-4344 |
| DOI: | 10.3390/catal10121395 |
| Popis: | Synthetic catalysts that could compete with enzymes in term of the catalytic efficiency but surpass them in stability have a great potential for the practical application. In this work, we have developed a novel kind of organic catalysts based on flow-through macroporous polymer monoliths containing catalytic centers that mimic the catalytic site of natural enzyme chymotrypsin. It is known that chymotrypsin catalytic center consists of L-serine, L-histidine, and L-aspartic acid and has specificity to C-terminal residues of hydrophobic amino acids (L-phenylalanine, L-tyrosine, and L-tryptophan). In this paper, we have prepared the macroporous polymer monoliths bearing grafted polymer layer on their surface. The last one was synthesized via copolymerization of N-methacryloyl-L-serine, N-methacryloyl-L-histidine, and N-methacryloyl-L-aspartic acid. The spatial orientation of amino acids in the polymer layer, generated on the surface of monolithic framework, was achieved by coordinating amino acid-polymerizable derivatives with cobalt (II) ions without substrate-mimicking template and with its use. The conditions for the preparation of mimic materials were optimized to achieve a mechanically stable system. Catalytic properties of the developed systems were evaluated towards the hydrolysis of ester bond in a low molecular substrate and compared to the results of using chymotrypsin immobilized on the surface of a similar monolithic framework. The effect of flow rate increase and temperature elevation on the hydrolysis efficiency were evaluated for both mimic monolith and column with immobilized enzyme. |
| Databáze: | OpenAIRE |
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