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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gitel'son I.I., Tikhomirov A.A., Parshina O.V., Ushakova S.A., Kalacheva G.S.
Заглавие : Volatile metabolites and external CO2 exchange of wheat cenoses under optimal conditions and thermal stress
Место публикации : Applied Biochemistry and Microbiology. - 2002. - Vol. 38, Is. 1. - С. 78-82. - ISSN 00036838 (ISSN) , DOI 10.1023/A:1013212907872
Ключевые слова (''Своб.индексиров.''): carbon dioxide--volatile agent--article--biosynthesis--carbon dioxide transport--chemical composition--concentration (parameters)--controlled study--cultivar--metabolite--nonhuman--photosynthesis--photosynthetically active radiation--plant metabolism--qualitative analysis--quantitative analysis--stress--temperature sensitivity--thermal exposure--thermostability--wheat--rickettsia sp. par--triticum--triticum aestivum
Аннотация: The effects of elevated temperature (35 and 45В°C) on photosynthesis, respiration, and both the qualitative and quantitative compositions of volatile emissions (VE) of wheat (Triticum aestuvum L. cultivar 232) cenoses at light intensities of 70, 150, or 240 W/m2 of photosynthetically available radiation (PAR) were studied. At a PAR of 240 W/m2, the thermal stabilities of photosynthesis and respiration increased at 35В°C and decreased at 45В°C. Elevated temperatures nonuniformly changed the rates and direction of VE syntheses. In this process, the highest increase in VE evolution was observed at 70 W/m2 and 35В°C; the lowest, at 240 W/m2. In addition, the concentrations and composition of VE during the repair period differed from the initial values.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., TROFIMOV K.P., SANDALOV T.P., VYSOTSKII E.S.
Заглавие : EFFECT OF TEMPERATURE ON ACTIVITY AND STABILITY OF OBELIN
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 7. - С. 717-724. - 8. - ISSN 0006-2979
Примечания : Cited References: 15
Предметные рубрики: CA-2+
PHOTOPROTEINS
INDICATORS
Ключевые слова (''Своб.индексиров.''): photoproteins--obelin--activation energy--thermoinactivation--thermostability
Аннотация: The temperature dependence of bioluminescent activity of the Ca2+-activated photoprotein obelin from the hydroid polyp Obelia longissima and thermoinactivation of this protein at different concentrations of (NH4)2SO4 have been studied. The maximal intensity of luminescence of obelin was observed at 4-15-degrees-C. The activity of the photoprotein is completely stable to storage for 3 days at room temperature. Increasing the temperature to 40-degrees-C resulted in a 25-30% loss of enzyme activity in 1 h. The presence of ammonium sulfate during heating stabilizes the activity of obelin. Two breaks, at 11 +/- 3-degrees-C and 47 +/- 3-degrees-C, are observed in the Arrhenius plot of the first-order rate constant of the luminescence decay. The bioluminescent curves of obelin are biphasic in the temperature range 10-40-degrees-C. It is assumed that obelin may exist in two kinetically distinct conformers (active and inactive) whose ratio is temperature dependent.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Vysotski E.S., Westphal A.H., van Mierlo CPM, van Berkel WJH
Заглавие : Ligand binding and conformational states of the photoprotein obelin
Колич.характеристики :7 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2012. - Vol. 586, Is. 23. - С. 4173-4179. - ISSN 0014-5793, DOI 10.1016/j.febslet.2012.10.015
Примечания : Cited References: 24. - The work was supported by RFBR grant 12-04-00131, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.058), by the Program "Molecular and Cellular Biology" of RAS. The Wageningen University Sandwich PhD-Fellowship Program supported E.V.E.
Предметные рубрики: RECOMBINANT OBELIN
CRYSTAL-STRUCTURE
LIGHT-EMISSION
APO-AEQUORIN
BIOLUMINESCENCE
COELENTERAZINE
LUMINESCENCE
STABILITY
ANGSTROM
PROTEINS
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--photoprotein--thermostability
Аннотация: Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism ( CD) data show that the various ligand-dependent conformational states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L. P., Natashin P. V., Malikova N. P., Niu F., Pu M., Vysotski E. S., Liu Z.-J.
Заглавие : All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin
Место публикации : J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - С. 57-66. - ISSN 10111344 (ISSN) , DOI 10.1016/j.jphotobiol.2015.11.012
Ключевые слова (''Своб.индексиров.''): aequorin--bioluminescence--calcium--coelenterazine--obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Markova, Svetlana V., Vysotski, Eugene S.
Заглавие : The novel extremely psychrophilic luciferase from Metridia longa: Properties of a high-purity protein produced in insect cells
Колич.характеристики :7 с
Коллективы : Bayer AG (Germany); Russian Academy of Sciences [01201351504]; RFBR; Government of Krasnoyarsk Territory [16-44-242099]
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2017. - Vol. 483, Is. 1. - С. 772-778. - ISSN 0006-291X, DOI 10.1016/j.bbrc.2016.12.067. - ISSN 1090-2104(eISSN)
Примечания : Cited References:24. - The cloning of cDNAs encoding MLuc2 isoforms of M. longa was supported by Bayer AG (Germany) and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 01201351504); all other studies were funded by RFBR and Government of Krasnoyarsk Territory according to the research project No. 16-44-242099.
Предметные рубрики: CDNA CLONING
EXPRESSION
ENZYME
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--bioluminescent reporter--psychrophilic--enzyme--molecular adaptation
Аннотация: The bright bioluminescence of copepod Metridia longa is conditioned by a small secreted coelenterazinedependent luciferase (MLuc). To date, three isoforms of MLuc differing in length, sequences, and some properties were cloned and successfully applied as high sensitive bioluminescent reporters. In this work, we report cloning of a novel group of genes from M. longa encoding extremely psychrophilic isoforms of MLuc (MLuc2-type). The novel isoforms share only similar to 54-64% of protein sequence identity with the previously cloned isoforms and, consequently, are the product of a separate group of paralogous genes. The MLuc2 isoform with consensus sequence was produced as a natively folded protein using baculovirus/ insect cell expression system, purified, and characterized. The MLuc2 displays a very high bioluminescent activity and high thermostability similar to those of the previously characterized M. longa luciferase isoform MLuc7. However, in contrast to MLuc7 revealing the highest activity at 12-17 degrees C and 0.5 M NaCl, the bioluminescence optima of MLuc2 isoforms are at similar to 5 degrees C and 1 M NaCl. The MLuc(2) adaptation to cold is also accompanied by decrease of melting temperature and affinity to substrate suggesting a more conformational flexibility of a protein structure. The luciferase isoforms with different temperature optima may provide adaptability of the M. longa bioluminescence to the changes of water temperature during diurnal vertical migrations. (C) 2016 Elsevier Inc. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Puzyr A. P., Medvedeva S. E., Artemenko K. S., Bondar V. S.
Заглавие : Luminescence of cold extracts from mycelium of luminous basidiomycetes during long-term storage
Место публикации : Curr. Res. Environ. Appl. Mycol. J. Fungal: Beijing Academy of Agriculture and Forestry Sciences, Institute of Plant and Environment Protection, 2017. - Vol. 7, Is. 3. - С. 227-235. - ISSN 22292225 (ISSN) , DOI 10.5943/cream/7/3/9
Ключевые слова (''Своб.индексиров.''): armillaria borealis--kinetics of luminescence--lyophilic preparations--mycena citricolor--neonothopanus nambi
Аннотация: Cold extracts with high activities of enzymes of luminescent reaction were prepared from mycelia of luminous fungi Armillaria borealis IBSO 2328, Mycena citricolor IBSO 2331, and Neonothopanus nambi IBSO 2391. The authors describe techniques of preparing cold extracts with high levels of luminescence from mycelial biomass of different species of luminous basidiomycetes. The investigation of cold extracts showed that in experiments with freezing and thawing of the samples as well as in experiments with lyophilization followed by dissolution of the dry samples, the levels of enzyme activity were high, with in vitro luminescence exhibited after addition of NADPH and the hot extract containing the substrate. High activity levels of the enzymes of luminescent reaction were measured in lyophilized cold extracts stored over three years. In lyophilized preparations, the enzymes of luminescent reaction had high thermostability, even when dry preparations of cold extracts were exposed to a temperature of 100°C for 60 minutes. © Beijing Academy of Agriculture and Forestry Sciences.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova, Svetlana V., Larionova, Marina D., Vysotski, Eugene S.
Заглавие : Shining Light on the Secreted Luciferases of Marine Copepods: Current Knowledge and Applications.
Место публикации : Photochemistry and photobiology. - 2018. - ISSN 1751-1097, DOI 10.1111/php.13077
Аннотация: Copepod luciferases - a family of small secretory proteins of 18.4-24.3 kDa, including a signal peptide, are responsible for bright secreted bioluminescence of some marine copepods. The copepod luciferases use coelenterazine as a substrate to produce blue light in a simple oxidation reaction without any additional cofactors. They do not share sequence or structural similarity with other identified bioluminescent proteins including coelenterazine-dependent Renilla and Oplophorus luciferases. The small size, strong luminescence activity and high stability, including thermostability, make secreted copepod luciferases very attractive candidates as reporter proteins which are particularly useful for nondisruptive reporter assays and for high-throughput format. The most known and extensively investigated representatives of this family are the first cloned GpLuc and MLuc luciferases from copepods Gaussia princeps and Metridia longa, respectively. Immediately after cloning these homologous luciferases were successfully applied as bioluminescent reporters in vivo and in vitro, and since then the scope of their applications continues to grow. This review is an attempt to systemize and critically evaluate the data scattered through numerous articles regarding the main structural features of copepod luciferases, their luminescent and physicochemical properties. We also review the main trends of their application as bioluminescent reporters in cell and molecular biology. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bakayan A., Picaud S., Malikova N. P., Tricoire L., Lambolez B., Vysotski E. S., Peyrieras N.
Заглавие : Redquorinxs mutants with enhanced calcium sensitivity and bioluminescence output efficiently report cellular and neuronal network activities
Место публикации : Int. J. Mol. Sci.: MDPI AG, 2020. - Vol. 21, Is. 21. - Ст.7846. - С. 1-22. - ISSN 16616596 (ISSN), DOI 10.3390/ijms21217846
Аннотация: Considerable efforts have been focused on shifting the wavelength of aequorin Ca2+? dependent blue bioluminescence through fusion with fluorescent proteins. This approach has notably yielded the widely used GFP?aequorin (GA) Ca2+ sensor emitting green light, and tdTomato-aequorin (Redquorin), whose bioluminescence is completely shifted to red, but whose Ca2+ sensitivity is low. In the present study, the screening of aequorin mutants generated at twenty?four amino acid positions in and around EF?hand Ca2+?binding domains resulted in the isolation of six aequorin single or double mutants (AequorinXS) in EF2, EF3, and C?terminal tail, which exhibited markedly higher Ca2+ sensitivity than wild?type aequorin in vitro. The corresponding Redquorin mutants all showed higher Ca2+ sensitivity than wild?type Redquorin, and four of them (RedquorinXS) matched the Ca2+ sensitivity of GA in vitro. RedquorinXS mutants exhibited unaltered thermostability and peak emission wavelengths. Upon stable expression in mammalian cell line, all RedquorinXS mutants reported the activation of the P2Y2 receptor by ATP with higher sensitivity and assay robustness than wt?Redquorin, and one, RedquorinXS?Q159T, outperformed GA. Finally, wide?field bioluminescence imaging in mouse neocortical slices showed that RedquorinXS?Q159T and GA similarly reported neuronal network activities elicited by the removal of extracellular Mg2+. Our results indicate that RedquorinXS?Q159T is a red light?emitting Ca2+ sensor suitable for the monitoring of intracellular signaling in a variety of applications in cells and tissues, and is a promising candidate for the transcranial monitoring of brain activities in living mice. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bakayan, Adil, Picaud, Sandrine, Malikova, Natalia P., Tricoire, Ludovic, Lambolez, Bertrand, Vysotski, Eugene S., Peyrieras, Nadine
Заглавие : RedquorinXS Mutants with Enhanced Calcium Sensitivity and Bioluminescence Output Efficiently Report Cellular and Neuronal Network Activities
Колич.характеристики :20 с
Коллективы : Centre National de la Recherche ScientifiqueCentre National de la Recherche Scientifique (CNRS); Agence Nationale de la RechercheFrench National Research Agency (ANR) [ANR-10-INBS-04, ANR-11-EQPX-029]; Fondation pour la Recherche sur le Cerveau/Rotary Club de France; RFBRRussian Foundation for Basic Research (RFBR) [20-04-00085]
Место публикации : Int. J. Mol. Sci.: MDPI, 2020. - Vol. 21, Is. 21. - Ст.7846. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms21217846
Примечания : Cited References:53. - This work was supported by grants from Centre National de la Recherche Scientifique (AAP Prematuration CNRS 2016, to A.B. and N.P.; equipment transfer to S.P. and B.L.), from Agence Nationale de la Recherche (AAP Prematuration FCS/IDEX Paris Saclay, to A.B. and N.P., France BioImaging infrastructure ANR-10-INBS-04, ANR-11-EQPX-029 to N.P.), from Fondation pour la Recherche sur le Cerveau/Rotary Club de France (B.L.), and from RFBR (project number 20-04-00085 to N.P.M. and E.S.V.). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Предметные рубрики: IN-VIVO
PHOTOPROTEIN AEQUORIN
CA2+-REGULATED PHOTOPROTEINS
SPREADING
Аннотация: Considerable efforts have been focused on shifting the wavelength of aequorin Ca2+-dependent blue bioluminescence through fusion with fluorescent proteins. This approach has notably yielded the widely used GFP-aequorin (GA) Ca2+ sensor emitting green light, and tdTomato-aequorin (Redquorin), whose bioluminescence is completely shifted to red, but whose Ca2+ sensitivity is low. In the present study, the screening of aequorin mutants generated at twenty-four amino acid positions in and around EF-hand Ca2+-binding domains resulted in the isolation of six aequorin single or double mutants (AequorinXS) in EF2, EF3, and C-terminal tail, which exhibited markedly higher Ca2+ sensitivity than wild-type aequorin in vitro. The corresponding Redquorin mutants all showed higher Ca2+ sensitivity than wild-type Redquorin, and four of them (RedquorinXS) matched the Ca2+ sensitivity of GA in vitro. RedquorinXS mutants exhibited unaltered thermostability and peak emission wavelengths. Upon stable expression in mammalian cell line, all RedquorinXS mutants reported the activation of the P2Y2 receptor by ATP with higher sensitivity and assay robustness than wt-Redquorin, and one, RedquorinXS-Q159T, outperformed GA. Finally, wide-field bioluminescence imaging in mouse neocortical slices showed that RedquorinXS-Q159T and GA similarly reported neuronal network activities elicited by the removal of extracellular Mg2+. Our results indicate that RedquorinXS-Q159T is a red light-emitting Ca2+ sensor suitable for the monitoring of intracellular signaling in a variety of applications in cells and tissues, and is a promising candidate for the transcranial monitoring of brain activities in living mice.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Volova T., Kiselev E., Nemtsev I., Lukyanenko А., Sukovatyi A., Kuzmin A., Ryltseva G., Shishatskaya E.
Заглавие : Properties of degradable polyhydroxyalkanoates with different monomer compositions
Место публикации : Int. J. Biol. Macromol.: Elsevier B.V., 2021. - Vol. 182. - С. 98-114. - ISSN 01418130 (ISSN), DOI 10.1016/j.ijbiomac.2021.04.008
Аннотация: Purpose: To synthesize and investigate polyhydroxyalkanoates (PHAs) with different monomer composition and percentages and polymer films prepared from them. Results: Various PHAs: homopolymer poly-3-hydroxybutyrate P(3HB) and 2-, 3-, and 4-component copolymers comprising various combinations of 3-hydroxybutyrate (3HB), 3-hydroxyvalerate (3HV), 4-hydroxybutyrate (4HB), and 3-hydroxyhexanoate (3HHx) monomers were synthesized under specialized conditions. Relationships were found between the monomer composition of PHAs and their molecular-weight and thermal properties and degree of crystallinity. All copolymers had decreased weight average molecular weights, Mw (to 390–600 kDa), and increased values of polydispersity (3.2–4.6) compared to the P(3HB). PHA copolymers showed different thermal behavior: an insignificant decrease in Tmelt and the presence of the second peak in the melting region and changes in parameters of crystallization and glass transition. At the same time, they retained thermostability, and the difference between Tmelt and Tdegr was at least 100–120 °C. Incorporation of 4HB, 3HV, and 3HHx monomer units into the 3-hydroxybutyrate chain caused changes in the amorphous to crystalline ratio and decreased the degree of crystallinity (Cx) to 20–40%. According to the degree to which the monomers reduced crystallinity, they were ranked as follows: 4HB – 3HHx – 3HV. A unique set of films was produced; their surface properties and physical/mechanical properties were studied as dependent on PHA composition; monomers other than 3-hydroxybutyrate were found to enhance hydrophilicity, surface development, and elasticity of polymer films. Conclusion: An innovative set of PHA copolymers was synthesized and solution-cast films were prepared from them; the copolymers and films were investigated as dependent on polymer chemical composition. Results obtained in the present study contribute to the solution of a critical issue of producing degradable polymer materials. © 2021 Elsevier B.V.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Volova T., Kiselev E., Nemtsev I., Lukyanenko A., Sukovatyi A., Kuzmin A., Ryltseva G., Shishatskaya E.
Заглавие : Properties of degradable polyhydroxyalkanoates with different monomer compositions
Колич.характеристики :17 с
Коллективы : RFBRRussian Foundation for Basic Research (RFBR) [19-43-240012]; Ministry of Education and Science of the Russian FederationMinistry of Education and Science, Russian Federation [FSRZ-2020-0006]
Место публикации : Int. J. Biol. Macromol.: ELSEVIER, 2021. - Vol. 182. - С. 98-114. - ISSN 0141-8130, DOI 10.1016/j.ijbiomac.2021.04.008. - ISSN 1879-0003(eISSN)
Примечания : Cited References:106. - The part of the reported study on polymer synthesis and examinationwas funded by RFBR and KKRF [Grant No. 19-43-240012 "Biological and physical principles of production of new generation biomaterials"]. The work on production and investigation of polymer films was carried out as part of the State Assignment of the Ministry of Education and Science of the Russian Federation [Grant No. FSRZ-2020-0006].
Предметные рубрики: PALM KERNEL OIL
RALSTONIA-EUTROPHA
BIODEGRADABLE POLYMERS
Аннотация: Purpose: To synthesize and investigate polyhydroxyalkanoates (PHAs) with different monomer composition and percentages and polymer films prepared from them. Results: Various PHAs: homopolymer poly-3-hydroxybutyrate P(3HB) and 2-, 3-, and 4-component copolymers comprising various combinations of 3-hydroxybutyrate (3HB), 3-hydroxyvalerate (3HV), 4-hydroxybutyrate (4HB), and 3-hydroxyhexanoate (3HHx) monomers were synthesized under specialized conditions. Relationships were found between the monomer composition of PHAs and their molecular-weight and thermal properties and degree of crystallinity. All copolymers had decreased weight average molecular weights, Mw (to 390-600 kDa), and increased values of polydispersity (3.2-4.6) compared to the P(3HB). PHA copolymers showed different thermal behavior: an insignificant decrease in Tmelt and the presence of the second peak in the melting region and changes in parameters of crystallization and glass transition. At the same time, they retained thermostability, and the difference between Tmelt and Tdegr was at least 100-120 degrees C. Incorporation of 4HB, 3HV, and 3HHx monomer units into the 3-hydroxybutyrate chain caused changes in the amorphous to crystalline ratio and decreased the degree of crystallinity (Cx) to 20-40%. According to the degree to which the monomers reduced crystallinity, they were ranked as follows: 4HB - 3HHx - 3HV. A unique set of films was produced; their surface properties and physical/mechanical properties were studied as dependent on PHA composition; monomers other than 3hydroxybutyrate were found to enhance hydrophilicity, surface development, and elasticity of polymer films. Conclusion: An innovative set of PHA copolymers was synthesized and solution-cast films were prepared from them; the copolymers and films were investigated as dependent on polymer chemical composition. Results obtained in the present study contribute to the solution of a critical issue of producing degradable polymer materials. (C) 2021 Elsevier B.V. All rights reserved.
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