Stepanova, Mariia et al. published their research in Catalysts in 2020 |CAS: 2358-84-1

The Article related to chymotrypsin active site monolith, Catalysis, Reaction Kinetics, and Inorganic Reaction Mechanisms: Other and other aspects.Application In Synthesis of Oxybis(ethane-2,1-diyl) bis(2-methylacrylate)

Stepanova, Mariia; Solomakha, Olga; Ten, Daria; Tennikova, Tatiana; Korzhikova-Vlakh, Evgenia published an article in 2020, the title of the article was Flow-through macroporous polymer monoliths containing artificial catalytic centers mimicking chymotrypsin active site.Application In Synthesis of Oxybis(ethane-2,1-diyl) bis(2-methylacrylate) And the article contains the following content:

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 mech. stable system. Catalytic properties of the developed systems were evaluated towards the hydrolysis of ester bond in a low mol. 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. The experimental process involved the reaction of Oxybis(ethane-2,1-diyl) bis(2-methylacrylate)(cas: 2358-84-1).Application In Synthesis of Oxybis(ethane-2,1-diyl) bis(2-methylacrylate)

The Article related to chymotrypsin active site monolith, Catalysis, Reaction Kinetics, and Inorganic Reaction Mechanisms: Other and other aspects.Application In Synthesis of Oxybis(ethane-2,1-diyl) bis(2-methylacrylate)

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