Pub Date : 2024-07-11DOI: 10.3103/S0027131424700111
M. Ya. Melnikov, O. I. Gromov, V. I. Pergushov, D. A. Pomogailo, I. D. Sorokin
The review is dedicated to the photochemical reactions of radical cations (RC) of various organic oxygen-containing compounds stabilized in low-temperature matrices. The nature of RC and the products of their photochemical reactions has been established via quantum chemistry, electron paramagnetic resonance (EPR) and low-temperature optical spectroscopy. Depending on the structure of the precursor molecule, various mechanisms of photoconversion arise for these RC: charge transfer to matrix molecules, hydrogen atom and proton transfer, isomerization, dissociation. This study allowed us to posit that there is no correlation between the structure of the molecule of the precursor molecule and the variety of available phototransformation channels for the corresponding RC in frozen matrices.
{"title":"Photochemistry of Radical Cations of Some Organic Oxygen-Containing Compounds in Frozen Matrices","authors":"M. Ya. Melnikov, O. I. Gromov, V. I. Pergushov, D. A. Pomogailo, I. D. Sorokin","doi":"10.3103/S0027131424700111","DOIUrl":"10.3103/S0027131424700111","url":null,"abstract":"<p>The review is dedicated to the photochemical reactions of radical cations (RC) of various organic oxygen-containing compounds stabilized in low-temperature matrices. The nature of RC and the products of their photochemical reactions has been established via quantum chemistry, electron paramagnetic resonance (EPR) and low-temperature optical spectroscopy. Depending on the structure of the precursor molecule, various mechanisms of photoconversion arise for these RC: charge transfer to matrix molecules, hydrogen atom and proton transfer, isomerization, dissociation. This study allowed us to posit that there is no correlation between the structure of the molecule of the precursor molecule and the variety of available phototransformation channels for the corresponding RC in frozen matrices.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"147 - 155"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614276","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700184
L. A. Frank, V. V. Krasitskaya
This review presents the data on the structure of bioluminescent systems of marine animals that use coelenterazine-dependent luciferases as light-emitting proteins. It is shown that these luciferases and their genetic variants with new useful properties are successfully used as reporter molecules in a variety of analytical systems in vitro and in vivo due to the availability, stability, and high quantum yield of the reactions. Their application ensures a high level of sensitivity, simple design, and fast analysis.
{"title":"Coelenterazine-Dependent Luciferases: Properties and Application in Molecular Analysis","authors":"L. A. Frank, V. V. Krasitskaya","doi":"10.3103/S0027131424700184","DOIUrl":"10.3103/S0027131424700184","url":null,"abstract":"<p>This review presents the data on the structure of bioluminescent systems of marine animals that use coelenterazine-dependent luciferases as light-emitting proteins. It is shown that these luciferases and their genetic variants with new useful properties are successfully used as reporter molecules in a variety of analytical systems in vitro and in vivo due to the availability, stability, and high quantum yield of the reactions. Their application ensures a high level of sensitivity, simple design, and fast analysis.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"203 - 210"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614283","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700123
V. V. Shishova, E. S. Lokteva, G. S. Maksimov, K. I. Maslakov, I. Yu. Kaplin, S. V. Maksimov, E. V. Golubina
Pd/ZrO2 and Pd/ZrO2SiO2 catalysts prepared by wet impregnation and reduced with H2 under mild (30°C, aqueous suspension) or harsh (320°C) conditions are compared in the hydrodechlorination of the microecotoxicant diclofenac (DCF) in an aqueous solution at 30°С. According to the TPR and XPS data, the addition of SiO2 to the support reduces the degree of metal-support interaction and facilitates the reduction of palladium. Despite the lower Pd0 fraction, the Pd/ZrO2 catalyst is more active in the batch reactor: after reduction at 320°С, it slightly, and after mild reduction, significantly (7 times), exceeds Pd/ZrO2SiO2 in catalytic activity. XRD and TEM show a wider size distribution of palladium nanoparticles in the Pd/ZrO2 sample, while low-temperature N2 adsorption, XPS, and TPR demonstrated better accessibility of palladium on the Pd/ZrO2 surface due to the reduced decoration by the support components and increased pore size. These features explain the increased activity of Pd/ZrO2. Testing in the flow system demonstrated higher DCF conversion in the presence of catalysts reduced at 320°C and higher stability of Pd/ZrO2SiO2 compared to Pd/ZrO2. The stability is ensured by the increased reducibility of Pd2+ with H2 and by the developed surface of Pd/ZrO2SiO2, which prevents deactivation under the action of HCl released in hydrodechlorination.
{"title":"Hydrodechlorination of Diclofenac in an Aqueous Solution over Pd/ZrO2 and Pd/ZrO2SiO2 Catalysts","authors":"V. V. Shishova, E. S. Lokteva, G. S. Maksimov, K. I. Maslakov, I. Yu. Kaplin, S. V. Maksimov, E. V. Golubina","doi":"10.3103/S0027131424700123","DOIUrl":"10.3103/S0027131424700123","url":null,"abstract":"<div><p>Pd/ZrO<sub>2</sub> and Pd/ZrO<sub>2</sub>SiO<sub>2</sub> catalysts prepared by wet impregnation and reduced with H<sub>2</sub> under mild (30°C, aqueous suspension) or harsh (320°C) conditions are compared in the hydrodechlorination of the microecotoxicant diclofenac (DCF) in an aqueous solution at 30°С. According to the TPR and XPS data, the addition of SiO<sub>2</sub> to the support reduces the degree of metal-support interaction and facilitates the reduction of palladium. Despite the lower Pd<sup>0</sup> fraction, the Pd/ZrO<sub>2</sub> catalyst is more active in the batch reactor: after reduction at 320°С, it slightly, and after mild reduction, significantly (7 times), exceeds Pd/ZrO<sub>2</sub>SiO<sub>2</sub> in catalytic activity. XRD and TEM show a wider size distribution of palladium nanoparticles in the Pd/ZrO<sub>2</sub> sample, while low-temperature N<sub>2</sub> adsorption, XPS, and TPR demonstrated better accessibility of palladium on the Pd/ZrO<sub>2</sub> surface due to the reduced decoration by the support components and increased pore size. These features explain the increased activity of Pd/ZrO<sub>2</sub>. Testing in the flow system demonstrated higher DCF conversion in the presence of catalysts reduced at 320°C and higher stability of Pd/ZrO<sub>2</sub>SiO<sub>2</sub> compared to Pd/ZrO<sub>2</sub>. The stability is ensured by the increased reducibility of Pd<sup>2+</sup> with H<sub>2</sub> and by the developed surface of Pd/ZrO<sub>2</sub>SiO<sub>2</sub>, which prevents deactivation under the action of HCl released in hydrodechlorination.</p></div>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"156 - 169"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700214
Onur Ertik, Refiye Yanardag
In today’s world, disease rates are increasing day after day because of environmental factors, lifestyles and technology. Although there are many drugs for many diseases, people’s interest and demand for herbal products are increasing. So, plants that can be used in the treatment of diseases have to be researched scientifically. Neuraminidase belongs to a class of glycosyl hydrolases that release terminal sialic acid from glycoproteins, glycolipids and polysaccharides. Neuraminidases could be found in animals, microorganisms and viruses. They have an impact on pathogenicity. This enzyme which is required for viral replication is a surface glycoprotein in influenza types A and B. In this study, we examined the inhibitory effects of some plant extracts and chemical compounds on neuraminidase activity. The result of our experiments indicates that the neuraminidase inhibitory activities of plant extracts and chemical compounds increased in a dose-dependent manner. We can conclude that the plant extracts and chemicals/drugs can be used in pharmaceutical industries and drug treatment due to their neuraminidase inhibitory activities.
{"title":"Neuraminidase Inhibitory Activities of Some Alcoholic Plant Extracts and Chemical Compounds","authors":"Onur Ertik, Refiye Yanardag","doi":"10.3103/S0027131424700214","DOIUrl":"10.3103/S0027131424700214","url":null,"abstract":"<p>In today’s world, disease rates are increasing day after day because of environmental factors, lifestyles and technology. Although there are many drugs for many diseases, people’s interest and demand for herbal products are increasing. So, plants that can be used in the treatment of diseases have to be researched scientifically. Neuraminidase belongs to a class of glycosyl hydrolases that release terminal sialic acid from glycoproteins, glycolipids and polysaccharides. Neuraminidases could be found in animals, microorganisms and viruses. They have an impact on pathogenicity. This enzyme which is required for viral replication is a surface glycoprotein in influenza types A and B. In this study, we examined the inhibitory effects of some plant extracts and chemical compounds on neuraminidase activity. The result of our experiments indicates that the neuraminidase inhibitory activities of plant extracts and chemical compounds increased in a dose-dependent manner. We can conclude that the plant extracts and chemicals/drugs can be used in pharmaceutical industries and drug treatment due to their neuraminidase inhibitory activities.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"225 - 231"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141609522","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700172
N. V. Rastriga, N. L. Eremeev, D. A. Klimov, P. A. Levashov
In this study, an attempt is made to analyze the published data regarding the effectors of bacterial lysis in the presence of various bacteriolytic enzymes. Despite the differences between such enzymes, it is possible to identify certain general patterns of their action on a highly complex substrate—a living bacterial cell protected by a cell wall and additional complexes of biopolymers associated with it. Chicken and human lysozymes are the best known of these enzymes. They have some structural differences but are generally very similar in properties. Understanding the characteristics of the antibacterial action of bacteriolytic enzymes present both in medications and in the human immune system is extremely important for the development of new approaches to combat bacterial infections, including antibiotic-resistant ones. Moreover, certain logical and methodological approaches used to study bacteriolytic enzymes can be extremely useful for studying and describing other enzymes that affect complex polymer substrates in real biological situations.
{"title":"Regulation of Enzyme-Dependent Lysis of Microbial Cells: Is the Effector Target an Enzyme or Substrate?","authors":"N. V. Rastriga, N. L. Eremeev, D. A. Klimov, P. A. Levashov","doi":"10.3103/S0027131424700172","DOIUrl":"10.3103/S0027131424700172","url":null,"abstract":"<p>In this study, an attempt is made to analyze the published data regarding the effectors of bacterial lysis in the presence of various bacteriolytic enzymes. Despite the differences between such enzymes, it is possible to identify certain general patterns of their action on a highly complex substrate—a living bacterial cell protected by a cell wall and additional complexes of biopolymers associated with it. Chicken and human lysozymes are the best known of these enzymes. They have some structural differences but are generally very similar in properties. Understanding the characteristics of the antibacterial action of bacteriolytic enzymes present both in medications and in the human immune system is extremely important for the development of new approaches to combat bacterial infections, including antibiotic-resistant ones. Moreover, certain logical and methodological approaches used to study bacteriolytic enzymes can be extremely useful for studying and describing other enzymes that affect complex polymer substrates in real biological situations.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"195 - 202"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700159
T. A. Bogush, A. A. Basharina, I. P. Romanov, A. N. Grishanina, E. A. Bogush, A. M. Scherbakov, A. B. Ravcheeva, A. Lee, V. S. Kosorukov
A quantitative assessment of the expression of estrogen receptors alpha (ERα) is carried out in 115 samples of non-small cell lung cancer (NSCLC) by an immunofluorescent assay and flow cytometry. It is shown that a high level of ERα of ≥20% predicts a higher aggressiveness of NSCLC than at a low level of <20%: median survival based on a follow-up period of 78 months increases by 1.5 times; the risk of death is reduced by a factor of almost 2.0 (p = 0.04). The time to death increases on average by 18 months in about 20% of patients with a low ERα expression. The results validate the informative value of the immunofluorescence analysis and flow cytometry for quantifying the ERα expression and substantiate the prospects of antiestrogen therapy as a new option for NSCLC treatment, in particular, by analogy with breast cancer—in a long-term adjuvant therapy in ERα+ NSCLC patients.
{"title":"Immunofluorescence Analysis of Estrogen Receptors Alpha Expression in Non-Small Cell Lung Cancer Tissue","authors":"T. A. Bogush, A. A. Basharina, I. P. Romanov, A. N. Grishanina, E. A. Bogush, A. M. Scherbakov, A. B. Ravcheeva, A. Lee, V. S. Kosorukov","doi":"10.3103/S0027131424700159","DOIUrl":"10.3103/S0027131424700159","url":null,"abstract":"<p>A quantitative assessment of the expression of estrogen receptors alpha (ERα) is carried out in 115 samples of non-small cell lung cancer (NSCLC) by an immunofluorescent assay and flow cytometry. It is shown that a high level of ERα of ≥20% predicts a higher aggressiveness of NSCLC than at a low level of <20%: median survival based on a follow-up period of 78 months increases by 1.5 times; the risk of death is reduced by a factor of almost 2.0 (<i>p</i> = 0.04). The time to death increases on average by 18 months in about 20% of patients with a low ERα expression. The results validate the informative value of the immunofluorescence analysis and flow cytometry for quantifying the ERα expression and substantiate the prospects of antiestrogen therapy as a new option for NSCLC treatment, in particular, by analogy with breast cancer—in a long-term adjuvant therapy in ERα<sup>+</sup> NSCLC patients.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"182 - 188"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614414","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700196
N. K. Marynich, A. P. Savitsky
A search for amino acid residues, whose replacement could contribute to the optimal maturation of the moxSAASoti fluorescent protein at 37°C, is carried out. For many other fluorescent proteins, this characteristic was improved by chance through many rounds of random mutagenesis; however, we managed to find two positions, 74 and 125, which clearly affect the process of moxSAASoti maturation, which is verified by introducing substitutions at these positions by site-directed and site-saturation mutagenesis.
{"title":"Identification of “Hot Spots” to Improve Maturation of the moxSAASoti Fluorescent Protein at 37°C","authors":"N. K. Marynich, A. P. Savitsky","doi":"10.3103/S0027131424700196","DOIUrl":"10.3103/S0027131424700196","url":null,"abstract":"<p>A search for amino acid residues, whose replacement could contribute to the optimal maturation of the moxSAASoti fluorescent protein at 37°C, is carried out. For many other fluorescent proteins, this characteristic was improved by chance through many rounds of random mutagenesis; however, we managed to find two positions, 74 and 125, which clearly affect the process of moxSAASoti maturation, which is verified by introducing substitutions at these positions by site-directed and site-saturation mutagenesis.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"211 - 216"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700202
V. O. Ovsyannikov, A. Yu. Mikhailova, U. A. Budanova, Yu. L. Sebyakin
Recently, due to the growth in bacterial infections resistant to antibiotics, there is an urgent need for developing alternative antibacterial drugs. Alkyl-indolyl-L-lysines are a promising class of compounds; their amphiphilic structure is crucial in antimicrobial efficacy. A scheme is developed and five new derivatives of indolylbutyric and indolylacetic acids containing a polar amino acid residue with an ethylenediamine linker binding alkyl fragments with different lengths are synthesized. The antibacterial activity of the new amphiphiles against gram-positive and gram-negative bacterial strains is evaluated. The minimum binding energy of the synthesized compounds with human serum albumin (HSA) is determined by molecular docking. A lower affinity of the studied objects in comparison with control indolmycin is shown.
{"title":"Antibacterial Activity of Amphiphiles Based on Indolyl-3-Carboxylic Acids and L-Lysine with an Ethylenediamine Linker","authors":"V. O. Ovsyannikov, A. Yu. Mikhailova, U. A. Budanova, Yu. L. Sebyakin","doi":"10.3103/S0027131424700202","DOIUrl":"10.3103/S0027131424700202","url":null,"abstract":"<p>Recently, due to the growth in bacterial infections resistant to antibiotics, there is an urgent need for developing alternative antibacterial drugs. Alkyl-indolyl-L-lysines are a promising class of compounds; their amphiphilic structure is crucial in antimicrobial efficacy. A scheme is developed and five new derivatives of indolylbutyric and indolylacetic acids containing a polar amino acid residue with an ethylenediamine linker binding alkyl fragments with different lengths are synthesized. The antibacterial activity of the new amphiphiles against gram-positive and gram-negative bacterial strains is evaluated. The minimum binding energy of the synthesized compounds with human serum albumin (HSA) is determined by molecular docking. A lower affinity of the studied objects in comparison with control indolmycin is shown.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"217 - 224"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141609521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-11DOI: 10.3103/S0027131424700135
I. V. Grigoryan, V. V. Spiridonov, A. M. Adelyanov, Yu. A. Koksharov, K. V. Potapenkov, I. V. Taranov, G. B. Khomutov, A. A. Yaroslavov
This paper presents new colloidal systems that have prospects for use as carriers of medicinal compounds and are polymer complexes based on polyacrylic acid molecules of various molecular weights and biogenic polyamine, additionally modified with magnetic iron oxide nanoparticles. The main physicochemical characteristics of the resulting polycomplexes are determined. The possibility of incorporating a doxorubicin medicinal compound in the polycomplexes is demonstrated, and the magnetic properties of the polycomplexes functionalized with magnetic iron oxide nanoparticles are studied.
{"title":"New Magnetic Colloidal Systems Based on Biomimetic Polycomplexes","authors":"I. V. Grigoryan, V. V. Spiridonov, A. M. Adelyanov, Yu. A. Koksharov, K. V. Potapenkov, I. V. Taranov, G. B. Khomutov, A. A. Yaroslavov","doi":"10.3103/S0027131424700135","DOIUrl":"10.3103/S0027131424700135","url":null,"abstract":"<p>This paper presents new colloidal systems that have prospects for use as carriers of medicinal compounds and are polymer complexes based on polyacrylic acid molecules of various molecular weights and biogenic polyamine, additionally modified with magnetic iron oxide nanoparticles. The main physicochemical characteristics of the resulting polycomplexes are determined. The possibility of incorporating a doxorubicin medicinal compound in the polycomplexes is demonstrated, and the magnetic properties of the polycomplexes functionalized with magnetic iron oxide nanoparticles are studied.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"170 - 174"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/S0027131424700019
O. V. Maslova, O. V. Senko, N. A. Stepanov, I. V. Lyagin, E. N. Efremenko
Waste from the production and use of synthetic polymers is a serious problem. The development of enzymatic and microbial biocatalysts capable of degrading hard-to-decompose polymers seems to be one of the promising and environmentally oriented solutions to this problem. A possibility of combining biocatalysts (BCs)—enzymes and microbial cells—with metal catalysts is considered as a promising basis for the development of new hybrid chemobiocatalytic processes intended for the effective degradation of synthetic polymers (SPs).
{"title":"Biocatalysis in the Degradation of Synthetic Polymers","authors":"O. V. Maslova, O. V. Senko, N. A. Stepanov, I. V. Lyagin, E. N. Efremenko","doi":"10.3103/S0027131424700019","DOIUrl":"10.3103/S0027131424700019","url":null,"abstract":"<p>Waste from the production and use of synthetic polymers is a serious problem. The development of enzymatic and microbial biocatalysts capable of degrading hard-to-decompose polymers seems to be one of the promising and environmentally oriented solutions to this problem. A possibility of combining biocatalysts (BCs)—enzymes and microbial cells—with metal catalysts is considered as a promising basis for the development of new hybrid chemobiocatalytic processes intended for the effective degradation of synthetic polymers (SPs).</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 2","pages":"140 - 145"},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141513810","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}