Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

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Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site. / Stepanova, Mariia ; Solomakha , Olga ; Ten, Daria ; Tennikova, Tatiana ; Korzhikova-Vlakh, Evgenia .

In: Catalysts, Vol. 10, No. 12, 1395, 05.12.2020.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{adba79aebcff472ba13e3cfc8fcd3e8c,

title = "Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site",

abstract = "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.",

keywords = "Macroporous polymer monoliths, enzyme mimics, artificial catalytic centers, molecular imprinting, flow-through catalysis, catalyzed hydrolysis, Catalyzed hydrolysis, Artificial catalytic centers, Enzyme mimics, Molecular imprinting, Flow-through catalysis",

author = "Mariia Stepanova and Olga Solomakha and Daria Ten and Tatiana Tennikova and Evgenia Korzhikova-Vlakh",

note = "Publisher Copyright: {\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2020",

month = dec,

day = "5",

doi = "10.3390/catal10121395",

language = "English",

volume = "10",

journal = "Catalysts",

issn = "2073-4344",

publisher = "MDPI AG",

number = "12",

}

RIS

TY - JOUR

T1 - Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

AU - Stepanova, Mariia

AU - Solomakha , Olga

AU - Ten, Daria

AU - Tennikova, Tatiana

AU - Korzhikova-Vlakh, Evgenia

PY - 2020/12/5

Y1 - 2020/12/5

N2 - 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.

AB - 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.

KW - Macroporous polymer monoliths

KW - enzyme mimics

KW - artificial catalytic centers

KW - molecular imprinting

KW - flow-through catalysis

KW - catalyzed hydrolysis

KW - Catalyzed hydrolysis

KW - Artificial catalytic centers

KW - Enzyme mimics

KW - Molecular imprinting

KW - Flow-through catalysis

UR - http://www.scopus.com/inward/record.url?scp=85097254415&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/9eec75c6-2f1d-32ee-ab91-598b570055ed/

U2 - 10.3390/catal10121395

DO - 10.3390/catal10121395

M3 - Article

VL - 10

JO - Catalysts

JF - Catalysts

SN - 2073-4344

IS - 12

M1 - 1395

ER -

ID: 71461758