<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.3 20210610//EN" "JATS-journalpublishing1-3.dtd">
<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">meat</journal-id><journal-title-group><journal-title xml:lang="en">Theory and practice of meat processing</journal-title><trans-title-group xml:lang="ru"><trans-title>Теория и практика переработки мяса</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2414-438X</issn><issn pub-type="epub">2414-441X</issn><publisher><publisher-name>ФГБНУ «Федеральный научный центр пищевых систем им. В.М. Горбатова» РАН</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.21323/2414-438X-2022-7-2-76-82</article-id><article-id custom-type="elpub" pub-id-type="custom">meat-219</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>Статьи</subject></subj-group></article-categories><title-group><article-title>Technological approaches to the extraction and purification by ultrafiltration techniques of target protein molecules from animal tissues: a review</article-title><trans-title-group xml:lang="ru"><trans-title>Technological approaches to the extraction and purification by ultrafiltration techniques of target protein molecules from animal tissues: a review</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-1864-8115</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Kotenkova</surname><given-names>Е. A.</given-names></name><name name-style="western" xml:lang="en"><surname>Kotenkova</surname><given-names>E. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Elena A.  Kotenkova, Candidate of Technical Sciences, Research Scientist, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><bio xml:lang="en"><p>Elena A.  Kotenkova, Candidate of Technical Sciences, Research Scientist, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><email xlink:type="simple">lazovlena92@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-2719-9649</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Polishchuk</surname><given-names>E. K.</given-names></name><name name-style="western" xml:lang="en"><surname>Polishchuk</surname><given-names>E. K.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Ekaterina K.  Polishchuk, Research Engineer, Research Scientist, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><bio xml:lang="en"><p>Ekaterina K.  Polishchuk, Research Engineer, Research Scientist, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><email xlink:type="simple">e.politchuk@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>V. M. Gorbatov Federal Research Center for Food Systems</institution><country>Россия</country></aff><aff xml:lang="en"><institution>V. M. Gorbatov Federal Research Center for Food Systems</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>24</day><month>07</month><year>2022</year></pub-date><volume>7</volume><issue>2</issue><fpage>76</fpage><lpage>82</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Kotenkova E.A., Polishchuk E.K., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Kotenkova Е.A., Polishchuk E.K.</copyright-holder><copyright-holder xml:lang="en">Kotenkova E.A., Polishchuk E.K.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.meatjournal.ru/jour/article/view/219">https://www.meatjournal.ru/jour/article/view/219</self-uri><abstract><p>Effective isolation and purification of protein is a great challenge nowadays. The key aspect is protein stability and solubility, which primarily depend on protein structure and its amino acid sequence. Manipulations with pH and ionic strength are the first at  tempts to increase protein stability and solubility. Different additives that are allowed or prohibited in the food industry are applied for overcoming protein aggregation. Sugars, polyhydric alcohols and amino acids are the most attractive among them. Trehalose, glycerol, arginine, glycine and proline demonstrated outstanding properties that make them perspective for application during iso  lation and purification of proteins singly or in combination with each other or othercompounds. However, the algorithm of effective isolation and purification of protein could be significantly varied depending on its structure.</p><p> </p></abstract><trans-abstract xml:lang="ru"><p>Effective isolation and purification of protein is a great challenge nowadays. The key aspect is protein stability and solubility, which primarily depend on protein structure and its amino acid sequence. Manipulations with pH and ionic strength are the first at  tempts to increase protein stability and solubility. Different additives that are allowed or prohibited in the food industry are applied for overcoming protein aggregation. Sugars, polyhydric alcohols and amino acids are the most attractive among them. Trehalose, glycerol, arginine, glycine and proline demonstrated outstanding properties that make them perspective for application during iso  lation and purification of proteins singly or in combination with each other or othercompounds. However, the algorithm of effective isolation and purification of protein could be significantly varied depending on its structure.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>protein stability and solubility</kwd><kwd>kosmotrope</kwd><kwd>chaotrope</kwd><kwd>amino acid</kwd><kwd>sugar</kwd><kwd>polyhydric alcohol</kwd><kwd>detergent</kwd><kwd>osmolyte</kwd></kwd-group><kwd-group xml:lang="en"><kwd>protein stability and solubility</kwd><kwd>kosmotrope</kwd><kwd>chaotrope</kwd><kwd>amino acid</kwd><kwd>sugar</kwd><kwd>polyhydric alcohol</kwd><kwd>detergent</kwd><kwd>osmolyte</kwd></kwd-group><funding-group><funding-statement xml:lang="ru">The article was published as part of the research topic No. FNEN‑2019–0008 of the state assignment of the V. M. Gorbatov Federal Research Center for Food Systems of RAS</funding-statement><funding-statement xml:lang="en">The article was published as part of the research topic No. FNEN‑2019–0008 of the state assignment of the V. M. Gorbatov Federal Research Center for Food Systems of RAS</funding-statement></funding-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Dimitrov, D. S. (2012). Therapeutic proteins. Methods in Molecular Biology, 899, 1–26. https://doi.org/10.1007/978-1-61779-921-1_1</mixed-citation><mixed-citation xml:lang="en">Dimitrov, D. S. (2012). Therapeutic proteins. Methods in Molecular Biology, 899, 1–26. https://doi.org/10.1007/978-1-61779-921-1_1</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Sauna, Z. E., Lagassé, H. A. D., Alexaki, A., Simhadri, V. L., Katagiri, N. H., Jankowski, W. et.al. (2017). Recent advances in (therapeutic protein) drug development. F1000Research, 6, Article 113. https://doi.org/10.12688/f1000research.9970.1</mixed-citation><mixed-citation xml:lang="en">Sauna, Z. E., Lagassé, H. A. D., Alexaki, A., Simhadri, V. L., Katagiri, N. H., Jankowski, W. et.al. (2017). Recent advances in (therapeutic protein) drug development. F1000Research, 6, Article 113. https://doi.org/10.12688/f1000research.9970.1</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">de Marco, A., Berrow, N., Lebendiker, M., Garcia-Alai, M., Knauer, S. H., Lopez-Mendez, B. et al. (2021). Quality control of protein reagents for the improvement of research data reproducibility. Nature Communications, 12(1), Article 2795. https://doi.org/10.1038/s41467-021-23167-z</mixed-citation><mixed-citation xml:lang="en">de Marco, A., Berrow, N., Lebendiker, M., Garcia-Alai, M., Knauer, S. H., Lopez-Mendez, B. et al. (2021). Quality control of protein reagents for the improvement of research data reproducibility. Nature Communications, 12(1), Article 2795. https://doi.org/10.1038/s41467-021-23167-z</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Ismail, B. P., Senaratne-Lenagala, L., Stube, A., Brackenridge, A. (2020). Protein demand: Review of plant and animal proteins used in alternative protein product development and production. Animal Frontiers, 10(4), 53–63. https://doi.org/10.1093/af/vfaa040</mixed-citation><mixed-citation xml:lang="en">Ismail, B. P., Senaratne-Lenagala, L., Stube, A., Brackenridge, A. (2020). Protein demand: Review of plant and animal proteins used in alternative protein product development and production. Animal Frontiers, 10(4), 53–63. https://doi.org/10.1093/af/vfaa040</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Lukinova, E. A., Kotenkova, E. A., Polischuk, E. K. (2018). Influence of approaches to isolation of animal bioactive substances on antimicrobial action. Theory and Practice of Meat Processing, 3(3), 27–35. https://doi.org/10.21323/2414-438X-2018-3-3-27-35</mixed-citation><mixed-citation xml:lang="en">Lukinova, E. A., Kotenkova, E. A., Polischuk, E. K. (2018). Influence of approaches to isolation of animal bioactive substances on antimicrobial action. Theory and Practice of Meat Processing, 3(3), 27–35. https://doi.org/10.21323/2414-438X-2018-3-3-27-35</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Sanvictores, T., Farci, F. (2022). Biochemistry, Primary Protein Structure. StatPearls Publishing. Retrieved from https://www.ncbi.nlm.nih.gov/books/NBK564343/. Accessed April 14, 2022</mixed-citation><mixed-citation xml:lang="en">Sanvictores, T., Farci, F. (2022). Biochemistry, Primary Protein Structure. StatPearls Publishing. Retrieved from https://www.ncbi.nlm.nih.gov/books/NBK564343/. Accessed April 14, 2022</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Breda, A., Valadares, N. F., Norberto de Souza, O., Garratt, R. C. (2008). Protein Structure, Modelling and Applications. Chapter in a book: Bioinformatics in Tropical Disease Research: A Practical and Case-Study Approach. Bethesda (MD): National Center for Biotechnology Information (US). 2008. A06.</mixed-citation><mixed-citation xml:lang="en">Breda, A., Valadares, N. F., Norberto de Souza, O., Garratt, R. C. (2008). Protein Structure, Modelling and Applications. Chapter in a book: Bioinformatics in Tropical Disease Research: A Practical and Case-Study Approach. Bethesda (MD): National Center for Biotechnology Information (US). 2008. A06.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Sun, P. D., Foster, C. E., Boyington, J. C. (2004). Overview of Protein Structural and Functional Folds. Current Protocols in Protein Science, 35(1), 1711–171189. https://doi.org/10.1002/0471140864.ps1701s35</mixed-citation><mixed-citation xml:lang="en">Sun, P. D., Foster, C. E., Boyington, J. C. (2004). Overview of Protein Structural and Functional Folds. Current Protocols in Protein Science, 35(1), 1711–171189. https://doi.org/10.1002/0471140864.ps1701s35</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Aleksandrov, A., Polydorides, S., Archontis, G., Simonson, T. (2010). Predicting the acid/base behavior of proteins: A Constant-pH monte carlo approach with generalized born solvent. The Journal of Physical Chemistry B, 114(32), 10634–10648. https://doi.org/10.1021/jp104406x</mixed-citation><mixed-citation xml:lang="en">Aleksandrov, A., Polydorides, S., Archontis, G., Simonson, T. (2010). Predicting the acid/base behavior of proteins: A Constant-pH monte carlo approach with generalized born solvent. The Journal of Physical Chemistry B, 114(32), 10634–10648. https://doi.org/10.1021/jp104406x</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Audain, E., Ramos, Y., Hermjakob, H., Flower, D. R., PerezRiverol, Y. (2016). Accurate estimation of isoelectric point of protein and peptide based on amino acid sequences. Bioinformatics, 32(6), 821–827. https://doi.org/10.1093/bioinformatics/btv674</mixed-citation><mixed-citation xml:lang="en">Audain, E., Ramos, Y., Hermjakob, H., Flower, D. R., PerezRiverol, Y. (2016). Accurate estimation of isoelectric point of protein and peptide based on amino acid sequences. Bioinformatics, 32(6), 821–827. https://doi.org/10.1093/bioinformatics/btv674</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Nehete, J., Bhambar, R., Narkhede, M., Gawali, S. (2013). Natural proteins: Sources, isolation, characterization and applications. Pharmacognosy Reviews, 7(14), 107–116. https://doi.org/10.4103/0973–7847.120508</mixed-citation><mixed-citation xml:lang="en">Nehete, J., Bhambar, R., Narkhede, M., Gawali, S. (2013). Natural proteins: Sources, isolation, characterization and applications. Pharmacognosy Reviews, 7(14), 107–116. https://doi.org/10.4103/0973–7847.120508</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Verollet, R. (2008). A major step towards efficient sample preparation with bead-beating. BioTechniques, 44(6), 832–833. https://doi.org/10.2144/000112893</mixed-citation><mixed-citation xml:lang="en">Verollet, R. (2008). A major step towards efficient sample preparation with bead-beating. BioTechniques, 44(6), 832–833. https://doi.org/10.2144/000112893</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Burden, D. W. (2012). Guide to the Disruption of Biological Samples — 2012. Random Primers, 12, 1–25.</mixed-citation><mixed-citation xml:lang="en">Burden, D. W. (2012). Guide to the Disruption of Biological Samples — 2012. Random Primers, 12, 1–25.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Franca-Oliveira, G., Fornari, T., Hernández-Ledesma, B. (2021). A review on the extraction and processing of natural source-derived proteins through eco-innovative approaches. Processes, 9(9), Article 1626. https://doi.org/10.3390/pr9091626</mixed-citation><mixed-citation xml:lang="en">Franca-Oliveira, G., Fornari, T., Hernández-Ledesma, B. (2021). A review on the extraction and processing of natural source-derived proteins through eco-innovative approaches. Processes, 9(9), Article 1626. https://doi.org/10.3390/pr9091626</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Novák, P., Havlíček, V. (2016). Protein Extraction and Precipitation. Chapter in a book: Proteomic Profiling and Analytical Chemistry. Elsevier. 2016.</mixed-citation><mixed-citation xml:lang="en">Novák, P., Havlíček, V. (2016). Protein Extraction and Precipitation. Chapter in a book: Proteomic Profiling and Analytical Chemistry. Elsevier. 2016.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Yasothai, R., Giriprasad, R. (2015). Acid/Alkaline solublization method of processing protein. International Journal of Science, Environment and Technology, 4(1), 96–100.</mixed-citation><mixed-citation xml:lang="en">Yasothai, R., Giriprasad, R. (2015). Acid/Alkaline solublization method of processing protein. International Journal of Science, Environment and Technology, 4(1), 96–100.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Hani, F. M., Cole, A. E., Altman, E. (2019). The ability of salts to stabilize proteins in vivo or intracellularly correlates with the Hofmeister series of ions. International Journal of Biochemistry and Molecular Biology, 10(3), 23–31.</mixed-citation><mixed-citation xml:lang="en">Hani, F. M., Cole, A. E., Altman, E. (2019). The ability of salts to stabilize proteins in vivo or intracellularly correlates with the Hofmeister series of ions. International Journal of Biochemistry and Molecular Biology, 10(3), 23–31.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Sharpe, T. (2014). Preventing Protein Aggregation. Biozentrum Biophysics Facility. Retrieved from https://www.biozentrum.unibas.ch/fileadmin/redaktion/05_Facilities/01_Technology_Platforms/BF/Protocols/Preventing_Protein_Aggregation.pdf. Accessed April 19, 2022.</mixed-citation><mixed-citation xml:lang="en">Sharpe, T. (2014). Preventing Protein Aggregation. Biozentrum Biophysics Facility. Retrieved from https://www.biozentrum.unibas.ch/fileadmin/redaktion/05_Facilities/01_Technology_Platforms/BF/Protocols/Preventing_Protein_Aggregation.pdf. Accessed April 19, 2022.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Castro-Muñoz, R., García-Depraect, O., León-Becerril, E., Cassano, A., Conidi, C., Fíla, V. (2021). Recovery of proteinbased compounds from meat by-products by membrane-assisted separations: a review. Journal of Chemical Technology and Biotechnology, 96(11), 3025–3042. https://doi.org/10.1002/jctb.6824</mixed-citation><mixed-citation xml:lang="en">Castro-Muñoz, R., García-Depraect, O., León-Becerril, E., Cassano, A., Conidi, C., Fíla, V. (2021). Recovery of proteinbased compounds from meat by-products by membrane-assisted separations: a review. Journal of Chemical Technology and Biotechnology, 96(11), 3025–3042. https://doi.org/10.1002/jctb.6824</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Reig, M., Vecino, X., Cortina, J. L. (2021). Use of membrane technologies in dairy industry: An overview. Foods, 10(11), Article 2768. https://doi.org/10.3390/foods10112768</mixed-citation><mixed-citation xml:lang="en">Reig, M., Vecino, X., Cortina, J. L. (2021). Use of membrane technologies in dairy industry: An overview. Foods, 10(11), Article 2768. https://doi.org/10.3390/foods10112768</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Miron, S. M., Dutournié, P., Thabet, K., Ponche, A. (2019). Filtration of protein-based solutions with ceramic ultrafiltration membrane. Study of selectivity, adsorption, and protein denaturation. Comptes Rendus Chimie, 22(2–3), 198–205. https://doi.org/10.1016/j.crci.2018.09.011</mixed-citation><mixed-citation xml:lang="en">Miron, S. M., Dutournié, P., Thabet, K., Ponche, A. (2019). Filtration of protein-based solutions with ceramic ultrafiltration membrane. Study of selectivity, adsorption, and protein denaturation. Comptes Rendus Chimie, 22(2–3), 198–205. https://doi.org/10.1016/j.crci.2018.09.011</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Arakawa, T., Ejima, D., Akuta, T. (2017). Protein aggregation under high concentration/density state during chromatographic and ultrafiltration processes. International Journal of Biological Macromolecules, 95, 1153–1158. https://doi.org/10.1016/j.ijbiomac.2016.11.005</mixed-citation><mixed-citation xml:lang="en">Arakawa, T., Ejima, D., Akuta, T. (2017). Protein aggregation under high concentration/density state during chromatographic and ultrafiltration processes. International Journal of Biological Macromolecules, 95, 1153–1158. https://doi.org/10.1016/j.ijbiomac.2016.11.005</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Cromwell, M. E. M., Hilario, E., Jacobson, F. (2006). Protein aggregation and bioprocessing. The AAPS Journal, 8(3), E572– E579, Article 66. https://doi.org/10.1208/aapsj080366</mixed-citation><mixed-citation xml:lang="en">Cromwell, M. E. M., Hilario, E., Jacobson, F. (2006). Protein aggregation and bioprocessing. The AAPS Journal, 8(3), E572– E579, Article 66. https://doi.org/10.1208/aapsj080366</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Ratnaningsih, E., Reynard, R., Khoiruddin, K., Wenten, I. G., Boopathy, R. (2021). Recent advancements of UF-based separation for selective enrichment of proteins and bioactive peptides — A review. Applied Sciences, 11(3), Article 1078. https://doi.org/10.3390/app11031078</mixed-citation><mixed-citation xml:lang="en">Ratnaningsih, E., Reynard, R., Khoiruddin, K., Wenten, I. G., Boopathy, R. (2021). Recent advancements of UF-based separation for selective enrichment of proteins and bioactive peptides — A review. Applied Sciences, 11(3), Article 1078. https://doi.org/10.3390/app11031078</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Callahan, D. J., Stanley, B., Li, Y. (2014). Control of Protein Particle Formation During Ultrafiltration/Diafiltration Through Interfacial Protection. Journal of Pharmaceutical Sciences, 103(3), 862–869. https://doi.org/10.1002/jps.23861</mixed-citation><mixed-citation xml:lang="en">Callahan, D. J., Stanley, B., Li, Y. (2014). Control of Protein Particle Formation During Ultrafiltration/Diafiltration Through Interfacial Protection. Journal of Pharmaceutical Sciences, 103(3), 862–869. https://doi.org/10.1002/jps.23861</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Fernandez-Cerezo, L., Rayat, A. C. M. E., Chatel, A., Pollard, J. M., Lye, G. J., Hoare, M. (2020). The prediction of the operating conditions on the permeate flux and on protein aggregation during membrane processing of monoclonal antibodies. Journal of Membrane Science, 596, Article 117606. https://doi.org/10.1016/j.memsci.2019.117606</mixed-citation><mixed-citation xml:lang="en">Fernandez-Cerezo, L., Rayat, A. C. M. E., Chatel, A., Pollard, J. M., Lye, G. J., Hoare, M. (2020). The prediction of the operating conditions on the permeate flux and on protein aggregation during membrane processing of monoclonal antibodies. Journal of Membrane Science, 596, Article 117606. https://doi.org/10.1016/j.memsci.2019.117606</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Bondos, S. E., Bicknell, A. (2003). Detection and prevention of protein aggregation before, during, and after purification. Analytical Biochemistry, 316(2), 223–231. https://doi.org/10.1016/S0003-2697(03)00059-9</mixed-citation><mixed-citation xml:lang="en">Bondos, S. E., Bicknell, A. (2003). Detection and prevention of protein aggregation before, during, and after purification. Analytical Biochemistry, 316(2), 223–231. https://doi.org/10.1016/S0003-2697(03)00059-9</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Lebendiker, M., Danieli, T. (2014). Production of prone-to-aggregate proteins. FEBS Letters, 588(2), 236–246. https://doi.org/10.1016/j.febslet.2013.10.044</mixed-citation><mixed-citation xml:lang="en">Lebendiker, M., Danieli, T. (2014). Production of prone-to-aggregate proteins. FEBS Letters, 588(2), 236–246. https://doi.org/10.1016/j.febslet.2013.10.044</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Leibly, D. J., Nguyen, T. N., Kao, L. T., Hewitt, S. N., Barrett, L. K., van Voorhis, W. C. (2012). Stabilizing additives added during cell lysis aid in the solubilization of recombinant proteins. PLoS ONE, 7(12), Article e52482. https://doi.org/10.1371/journal.pone.0052482</mixed-citation><mixed-citation xml:lang="en">Leibly, D. J., Nguyen, T. N., Kao, L. T., Hewitt, S. N., Barrett, L. K., van Voorhis, W. C. (2012). Stabilizing additives added during cell lysis aid in the solubilization of recombinant proteins. PLoS ONE, 7(12), Article e52482. https://doi.org/10.1371/journal.pone.0052482</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Bhat, E. A., Abdalla, M., Rather, I. A. (2018). Key factors for successful protein purification and crystallization. Global Journal of Biotechnology and Biomaterial Science, 4(1), 001–007. https://doi.org/10.17352/gjbbs.000010</mixed-citation><mixed-citation xml:lang="en">Bhat, E. A., Abdalla, M., Rather, I. A. (2018). Key factors for successful protein purification and crystallization. Global Journal of Biotechnology and Biomaterial Science, 4(1), 001–007. https://doi.org/10.17352/gjbbs.000010</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Jahan, I., Nayeem, S. M. (2018). Effect of urea, arginine, and ethanol concentration on aggregation of 179CVNITV184 fragment of sheep prion protein. ACS Omega, 3(9), 11727–11741. https://doi.org/10.1021/acsomega.8b00875</mixed-citation><mixed-citation xml:lang="en">Jahan, I., Nayeem, S. M. (2018). Effect of urea, arginine, and ethanol concentration on aggregation of 179CVNITV184 fragment of sheep prion protein. ACS Omega, 3(9), 11727–11741. https://doi.org/10.1021/acsomega.8b00875</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., Panda, A. K. (2015). Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process. Microbial Cell Factories, 14(1), Article 41. https://doi.org/10.1186/s12934-015-0222-8</mixed-citation><mixed-citation xml:lang="en">Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., Panda, A. K. (2015). Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process. Microbial Cell Factories, 14(1), Article 41. https://doi.org/10.1186/s12934-015-0222-8</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Gifre-Renom, L., Cano-Garrido, O., Fàbregas, F., Roca-Pinilla, R., Seras-Franzoso, J., Ferrer-Miralles, N. et al. (2018). A new approach to obtain pure and active proteins from Lactococcus lactis protein aggregates. Scientific Reports, 8(1), Article 13917. https://doi.org/10.1038/s41598-018-32213-8</mixed-citation><mixed-citation xml:lang="en">Gifre-Renom, L., Cano-Garrido, O., Fàbregas, F., Roca-Pinilla, R., Seras-Franzoso, J., Ferrer-Miralles, N. et al. (2018). A new approach to obtain pure and active proteins from Lactococcus lactis protein aggregates. Scientific Reports, 8(1), Article 13917. https://doi.org/10.1038/s41598-018-32213-8</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Akhremko, A., Vasilevskaya, E., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscle tissue analysis. Potravinarstvo Slovak Journal of Food Sciences, 14, 595– 601. https://doi.org/10.5219/1380</mixed-citation><mixed-citation xml:lang="en">Akhremko, A., Vasilevskaya, E., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscle tissue analysis. Potravinarstvo Slovak Journal of Food Sciences, 14, 595– 601. https://doi.org/10.5219/1380</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">The Protein Man’s Blog | A Discussion of Protein Research. Tips for Preventing Protein Aggregation &amp; Loss of Protein Solubility. Retrieved from https://info.gbiosciences.com/blog/tipsfor-preventing-protein-aggregation-loss-of-protein-solubility. Accessed April 19, 2022.</mixed-citation><mixed-citation xml:lang="en">The Protein Man’s Blog | A Discussion of Protein Research. Tips for Preventing Protein Aggregation &amp; Loss of Protein Solubility. Retrieved from https://info.gbiosciences.com/blog/tipsfor-preventing-protein-aggregation-loss-of-protein-solubility. Accessed April 19, 2022.</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Liao, Y.-T., Manson, A. C., DeLyser, M. R., Noid, W. G., Cremer, P. S. (2017). Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine. Proceedings of the National Academy of Sciences, 114(10), 2479–2484. https://doi.org/10.1073/pnas.1614609114</mixed-citation><mixed-citation xml:lang="en">Liao, Y.-T., Manson, A. C., DeLyser, M. R., Noid, W. G., Cremer, P. S. (2017). Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine. Proceedings of the National Academy of Sciences, 114(10), 2479–2484. https://doi.org/10.1073/pnas.1614609114</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Acharyya, A., Shin, D., Troxler, T., Gai, F. (2020). Can glycine betaine denature proteins? Physical Chemistry Chemical Physics, 22(15), 7794–7802. https://doi.org/10.1039/d0cp00397b</mixed-citation><mixed-citation xml:lang="en">Acharyya, A., Shin, D., Troxler, T., Gai, F. (2020). Can glycine betaine denature proteins? Physical Chemistry Chemical Physics, 22(15), 7794–7802. https://doi.org/10.1039/d0cp00397b</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Singh, L. R., Dar, T. A., Rahman, S., Jamal, S., Ahmad, F. (2009). Glycine betaine may have opposite effects on protein stability at high and low pH values. Biochimica et Biophysica Acta (BBA) — Proteins and Proteomics, 1794(6), 929–935. https://doi.org/10.1016/j.bbapap.2009.02.005</mixed-citation><mixed-citation xml:lang="en">Singh, L. R., Dar, T. A., Rahman, S., Jamal, S., Ahmad, F. (2009). Glycine betaine may have opposite effects on protein stability at high and low pH values. Biochimica et Biophysica Acta (BBA) — Proteins and Proteomics, 1794(6), 929–935. https://doi.org/10.1016/j.bbapap.2009.02.005</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Chui, T. C. Y., Kim, W., Ramsheh, A. S., Yang, C. (2020). Glycine Betaine synthesis and transport Proteins, BetTIBA and ProPU, in Escherichia coli K12 do not confer Resistance to SDS-EDTA induced Outer Membrane Stress. Undergraduate Journal of Experimental Microbiology and Immunology, 25, 1–7. https://doi.org/10.14288/ujemi.v25i.193262</mixed-citation><mixed-citation xml:lang="en">Chui, T. C. Y., Kim, W., Ramsheh, A. S., Yang, C. (2020). Glycine Betaine synthesis and transport Proteins, BetTIBA and ProPU, in Escherichia coli K12 do not confer Resistance to SDS-EDTA induced Outer Membrane Stress. Undergraduate Journal of Experimental Microbiology and Immunology, 25, 1–7. https://doi.org/10.14288/ujemi.v25i.193262</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Li, J., Chen, J., An, L., Yuan, X., Yao, L. (2020). Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function. Communications Biology, 3(1), Article 528. https://doi.org/10.1038/s42003-020-01260-1</mixed-citation><mixed-citation xml:lang="en">Li, J., Chen, J., An, L., Yuan, X., Yao, L. (2020). Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function. Communications Biology, 3(1), Article 528. https://doi.org/10.1038/s42003-020-01260-1</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Schein, C. H. (1990). Solubility as a function of protein structure and solvent components. Nature Biotechnology, 8(4), 308– 317. https://doi.org/10.1038/nbt0490-308</mixed-citation><mixed-citation xml:lang="en">Schein, C. H. (1990). Solubility as a function of protein structure and solvent components. Nature Biotechnology, 8(4), 308– 317. https://doi.org/10.1038/nbt0490-308</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Jain, N. K., Roy, I. (2008). Effect of trehalose on protein structure. Protein Science, 18(1), 24–36. https://doi.org/10.1002/pro.3</mixed-citation><mixed-citation xml:lang="en">Jain, N. K., Roy, I. (2008). Effect of trehalose on protein structure. Protein Science, 18(1), 24–36. https://doi.org/10.1002/pro.3</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Rajan, R., Ahmed, S., Sharma, N., Kumar, N., Debas, A., Matsumura, K. (2021). Review of the current state of protein aggregation inhibition from a materials chemistry perspective: Special focus on polymeric materials. Materials Advances, 2(4), 1139– 1176. https://doi.org/10.1039/d0ma00760a</mixed-citation><mixed-citation xml:lang="en">Rajan, R., Ahmed, S., Sharma, N., Kumar, N., Debas, A., Matsumura, K. (2021). Review of the current state of protein aggregation inhibition from a materials chemistry perspective: Special focus on polymeric materials. Materials Advances, 2(4), 1139– 1176. https://doi.org/10.1039/d0ma00760a</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Olsson, C., Swenson, J. (2019). The role of disaccharides for protein–protein interactions — a SANS study. Molecular Physics, 117(22), 3408–3416. https://doi.org/10.1080/00268976.2019.1640400</mixed-citation><mixed-citation xml:lang="en">Olsson, C., Swenson, J. (2019). The role of disaccharides for protein–protein interactions — a SANS study. Molecular Physics, 117(22), 3408–3416. https://doi.org/10.1080/00268976.2019.1640400</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Lee, J. C., Timasheff, S. N. (1981). The stabilization of proteins by sucrose. The Journal of Biological Chemistry, 256(14), 7193–7201.</mixed-citation><mixed-citation xml:lang="en">Lee, J. C., Timasheff, S. N. (1981). The stabilization of proteins by sucrose. The Journal of Biological Chemistry, 256(14), 7193–7201.</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Zapadka, K. L., Becher, F. J., Gomes dos Santos, A. L., Jackson, S. E. (2017). Factors affecting the physical stability (aggregation) of peptide therapeutics. Interface Focus, 7(6), Article 20170030. https://doi.org/10.1098/rsfs.2017.0030</mixed-citation><mixed-citation xml:lang="en">Zapadka, K. L., Becher, F. J., Gomes dos Santos, A. L., Jackson, S. E. (2017). Factors affecting the physical stability (aggregation) of peptide therapeutics. Interface Focus, 7(6), Article 20170030. https://doi.org/10.1098/rsfs.2017.0030</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Vagenende, V., Yap, M. G. S., Trout, B. L. (2009). Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochemistry, 48(46), 11084–11096. https://doi.org/10.1021/bi900649t</mixed-citation><mixed-citation xml:lang="en">Vagenende, V., Yap, M. G. S., Trout, B. L. (2009). Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochemistry, 48(46), 11084–11096. https://doi.org/10.1021/bi900649t</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Hirai, M., Ajito, S., Sugiyama, M., Iwase, H., Takata, S., Shimizu, N. et al. (2018). Direct evidence for the effect of glycerol on protein hydration and thermal structural transition. Biophysical Journal, 115(2), 313–327. https://doi.org/10.1016/j.bpj.2018.06.005</mixed-citation><mixed-citation xml:lang="en">Hirai, M., Ajito, S., Sugiyama, M., Iwase, H., Takata, S., Shimizu, N. et al. (2018). Direct evidence for the effect of glycerol on protein hydration and thermal structural transition. Biophysical Journal, 115(2), 313–327. https://doi.org/10.1016/j.bpj.2018.06.005</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Petersen, S. B., Jonson, V., Fojan, P., Wimmer, R., Pedersen, S. (2004). Sorbitol prevents the self-aggregation of unfolded lysozyme leading to an up to 13 °C stabilisation of the folded form. Journal of Biotechnology, 114(3), 269–278. https://doi.org/10.1016/j.jbiotec.2004.07.004</mixed-citation><mixed-citation xml:lang="en">Petersen, S. B., Jonson, V., Fojan, P., Wimmer, R., Pedersen, S. (2004). Sorbitol prevents the self-aggregation of unfolded lysozyme leading to an up to 13 °C stabilisation of the folded form. Journal of Biotechnology, 114(3), 269–278. https://doi.org/10.1016/j.jbiotec.2004.07.004</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Soleymani, B., Mostafaie, A. (2019). Analysis of methods to improve the solubility of recombinant bovine sex determining region Y protein. Reports of Biochemistry and Molecular Biology, 8(3), 227–235.</mixed-citation><mixed-citation xml:lang="en">Soleymani, B., Mostafaie, A. (2019). Analysis of methods to improve the solubility of recombinant bovine sex determining region Y protein. Reports of Biochemistry and Molecular Biology, 8(3), 227–235.</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Alibolandi, M., Mirzahoseini, H. (2011). Chemical assistance in refolding of bacterial inclusion bodies. Biochemistry Research International, 2011, Article 631607. https://doi.org/10.1155/2011/631607</mixed-citation><mixed-citation xml:lang="en">Alibolandi, M., Mirzahoseini, H. (2011). Chemical assistance in refolding of bacterial inclusion bodies. Biochemistry Research International, 2011, Article 631607. https://doi.org/10.1155/2011/631607</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Jin, W., Xing, Z., Song, Y., Huang, C., Xu, X., Ghose, S. et al. (2019). Protein aggregation and mitigation strategy in low pH viral inactivation for monoclonal antibody purification. mAbs, 11(8), 1479–1491. https://doi.org/10.1080/19420862.2019.1658493</mixed-citation><mixed-citation xml:lang="en">Jin, W., Xing, Z., Song, Y., Huang, C., Xu, X., Ghose, S. et al. (2019). Protein aggregation and mitigation strategy in low pH viral inactivation for monoclonal antibody purification. mAbs, 11(8), 1479–1491. https://doi.org/10.1080/19420862.2019.1658493</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Xu, Q., Deng, H., Li, X., Quan, Z.-S. (2021). Application of amino acids in the structural modification of natural products: A review. Frontiers in Chemistry, 9, Article 650569. https://doi.org/10.3389/fchem.2021.650569</mixed-citation><mixed-citation xml:lang="en">Xu, Q., Deng, H., Li, X., Quan, Z.-S. (2021). Application of amino acids in the structural modification of natural products: A review. Frontiers in Chemistry, 9, Article 650569. https://doi.org/10.3389/fchem.2021.650569</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Shiraki, K., Kudou, M., Fujiwara, S., Imanaka, T., Takagi, M. (2002). Biophysical effect of amino acids on the prevention of protein aggregation. Journal of Biochemistry, 132(4), 591–595. https://doi.org/10.1093/oxfordjournals.jbchem.a003261</mixed-citation><mixed-citation xml:lang="en">Shiraki, K., Kudou, M., Fujiwara, S., Imanaka, T., Takagi, M. (2002). Biophysical effect of amino acids on the prevention of protein aggregation. Journal of Biochemistry, 132(4), 591–595. https://doi.org/10.1093/oxfordjournals.jbchem.a003261</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Das, U., Hariprasad, G., Ethayathulla, A. S., Manral, P., Das, T. K., Pasha, S. et al. (2007). Inhibition of protein aggregation: Supramolecular assemblies of Arginine hold the key. PLoS ONE, 2(11), Article e1176. https://doi.org/10.1371/journal.pone.0001176</mixed-citation><mixed-citation xml:lang="en">Das, U., Hariprasad, G., Ethayathulla, A. S., Manral, P., Das, T. K., Pasha, S. et al. (2007). Inhibition of protein aggregation: Supramolecular assemblies of Arginine hold the key. PLoS ONE, 2(11), Article e1176. https://doi.org/10.1371/journal.pone.0001176</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., Philo, J. S., Arakawa, T. (2004). Role of arginine in protein refolding, solubilization, and purification. Biotechnology Progress, 20(5), 1301– 1308. https://doi.org/10.1021/bp0498793</mixed-citation><mixed-citation xml:lang="en">Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., Philo, J. S., Arakawa, T. (2004). Role of arginine in protein refolding, solubilization, and purification. Biotechnology Progress, 20(5), 1301– 1308. https://doi.org/10.1021/bp0498793</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Shukla, D., Trout, B. L. (2010). Interaction of arginine with proteins and the mechanism by which it inhibits aggregation. The Journal of Physical Chemistry B, 114(42), 13426–13438. https://doi.org/10.1021/jp108399g</mixed-citation><mixed-citation xml:lang="en">Shukla, D., Trout, B. L. (2010). Interaction of arginine with proteins and the mechanism by which it inhibits aggregation. The Journal of Physical Chemistry B, 114(42), 13426–13438. https://doi.org/10.1021/jp108399g</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Shaikh, A. R., Shah, D. (2015). Arginine-Amino acid interactions and implications to protein solubility and aggregation. The Journal of Engineering Research, 12(2), 1–14. https://doi.org/10.24200/tjer.vol12iss2pp1-14</mixed-citation><mixed-citation xml:lang="en">Shaikh, A. R., Shah, D. (2015). Arginine-Amino acid interactions and implications to protein solubility and aggregation. The Journal of Engineering Research, 12(2), 1–14. https://doi.org/10.24200/tjer.vol12iss2pp1-14</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Varughese, M. M., Newman, J. (2012). Inhibitory effects of arginine on the aggregation of bovine insulin. Journal of Biophysics, 2012, Article 434289. https://doi.org/10.1155/2012/434289</mixed-citation><mixed-citation xml:lang="en">Varughese, M. M., Newman, J. (2012). Inhibitory effects of arginine on the aggregation of bovine insulin. Journal of Biophysics, 2012, Article 434289. https://doi.org/10.1155/2012/434289</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Wang, X.-T., Engel, P. C. (2009). An optimised system for refolding of human glucose 6-phosphate dehydrogenase. BMC Biotechnology, 9(1), Article 19. https://doi.org/10.1186/1472-6750-9-19</mixed-citation><mixed-citation xml:lang="en">Wang, X.-T., Engel, P. C. (2009). An optimised system for refolding of human glucose 6-phosphate dehydrogenase. BMC Biotechnology, 9(1), Article 19. https://doi.org/10.1186/1472-6750-9-19</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Kheddo, P. (2016). Effect of Arginine Glutamate on Protein Aggregation in Biopharmaceutical Formulation. Retrieved from https://www.research.manchester.ac.uk/portal/files/63039132/FULL_TEXT.PDF. Accessed April 20, 2022.</mixed-citation><mixed-citation xml:lang="en">Kheddo, P. (2016). Effect of Arginine Glutamate on Protein Aggregation in Biopharmaceutical Formulation. Retrieved from https://www.research.manchester.ac.uk/portal/files/63039132/FULL_TEXT.PDF. Accessed April 20, 2022.</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Golovanov, A. P., Hautbergue, G. M., Wilson, S. A., Lian, L.-Y. (2004). A simple method for improving protein solubility and longterm stability. Journal of the American Chemical Society, 126(29), 8933–8939. https://doi.org/10.1021/ja049297h</mixed-citation><mixed-citation xml:lang="en">Golovanov, A. P., Hautbergue, G. M., Wilson, S. A., Lian, L.-Y. (2004). A simple method for improving protein solubility and longterm stability. Journal of the American Chemical Society, 126(29), 8933–8939. https://doi.org/10.1021/ja049297h</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Shukla, D., Trout, B. L. (2011). Understanding the synergistic effect of arginine and glutamic acid mxtures on protein solubility. The Journal of Physical Chemistry B, 115(41), 11831–11839. https://doi.org/10.1021/jp204462t</mixed-citation><mixed-citation xml:lang="en">Shukla, D., Trout, B. L. (2011). Understanding the synergistic effect of arginine and glutamic acid mxtures on protein solubility. The Journal of Physical Chemistry B, 115(41), 11831–11839. https://doi.org/10.1021/jp204462t</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Platts, L., Falconer, R. J. (2015). Controlling protein stability: Mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins. International Journal of Pharmaceutics, 486(1–2), 131–135. https://doi.org/10.1016/j.ijpharm.2015.03.051</mixed-citation><mixed-citation xml:lang="en">Platts, L., Falconer, R. J. (2015). Controlling protein stability: Mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins. International Journal of Pharmaceutics, 486(1–2), 131–135. https://doi.org/10.1016/j.ijpharm.2015.03.051</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Imura, Y., Tagawa, T., Miyamoto, Y., Nonoyama, S., Sumichika, H., Fujino, Y.et al. (2021). Washing with alkaline solutions in protein A purification improves physicochemical properties of monoclonal antibodies. Scientific Reports, 11(1), Article 1827. https://doi.org/10.1038/s41598-021-81366-6</mixed-citation><mixed-citation xml:lang="en">Imura, Y., Tagawa, T., Miyamoto, Y., Nonoyama, S., Sumichika, H., Fujino, Y.et al. (2021). Washing with alkaline solutions in protein A purification improves physicochemical properties of monoclonal antibodies. Scientific Reports, 11(1), Article 1827. https://doi.org/10.1038/s41598-021-81366-6</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang, Y.-B., Howitt, J., McCorkle, S., Lawrence, P., Springer, K., Freimuth, P. (2004). Protein aggregation during overexpression limited by peptide extensions with large net negative charge. Protein Expression and Purification, 36(2), 207–216. https://doi.org/10.1016/j.pep.2004.04.020</mixed-citation><mixed-citation xml:lang="en">Zhang, Y.-B., Howitt, J., McCorkle, S., Lawrence, P., Springer, K., Freimuth, P. (2004). Protein aggregation during overexpression limited by peptide extensions with large net negative charge. Protein Expression and Purification, 36(2), 207–216. https://doi.org/10.1016/j.pep.2004.04.020</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Lopez, E., Scott, N. E., Wines, B. D., Hogarth, P. M., Wheatley, A. K., Kent, S. J. et al. (2019). Low pH exposure during immunoglobulin G purification methods results in aggregates that avidly bind Fcγ receptors: Implications for measuring Fc dependent antibody functions. Frontiers in Immunology, 10, Article 2415. https://doi.org/10.3389/fimmu.2019.02415</mixed-citation><mixed-citation xml:lang="en">Lopez, E., Scott, N. E., Wines, B. D., Hogarth, P. M., Wheatley, A. K., Kent, S. J. et al. (2019). Low pH exposure during immunoglobulin G purification methods results in aggregates that avidly bind Fcγ receptors: Implications for measuring Fc dependent antibody functions. Frontiers in Immunology, 10, Article 2415. https://doi.org/10.3389/fimmu.2019.02415</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Chen, S., Manabe, Y., Minamoto, N., Saiki, N., Fukase, K. (2016). Development of a simple assay system for protein-stabilizing efficiency based on hemoglobin protection against denaturation and measurement of the cooperative effect of mixing protein stabilizers. Bioscience, Biotechnology, and Biochemistry, 80(10), 1874–1878. https://doi.org/10.1080/09168451.2016.1189317</mixed-citation><mixed-citation xml:lang="en">Chen, S., Manabe, Y., Minamoto, N., Saiki, N., Fukase, K. (2016). Development of a simple assay system for protein-stabilizing efficiency based on hemoglobin protection against denaturation and measurement of the cooperative effect of mixing protein stabilizers. Bioscience, Biotechnology, and Biochemistry, 80(10), 1874–1878. https://doi.org/10.1080/09168451.2016.1189317</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Samuel, D., Kumar, T.K.S., Ganesh, G., Jayaraman, G., Yang, P.-W., Chang, M.-M. et. al. (2008). Proline inhibits aggregation during protein refolding. Protein Science, 9(2), 344–352. https://doi.org/10.1110/ps.9.2.344</mixed-citation><mixed-citation xml:lang="en">Samuel, D., Kumar, T.K.S., Ganesh, G., Jayaraman, G., Yang, P.-W., Chang, M.-M. et. al. (2008). Proline inhibits aggregation during protein refolding. Protein Science, 9(2), 344–352. https://doi.org/10.1110/ps.9.2.344</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Kumat, T. K. S., Samuel, D., Jayaraman, G., Srimathi, T., Yu, C. (1998). The role of proline in the prevention of aggregation during protein folding in vitro. Biochemistry and Molecular Biology International, 46(3), 509–517.</mixed-citation><mixed-citation xml:lang="en">Kumat, T. K. S., Samuel, D., Jayaraman, G., Srimathi, T., Yu, C. (1998). The role of proline in the prevention of aggregation during protein folding in vitro. Biochemistry and Molecular Biology International, 46(3), 509–517.</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Gentiluomo, L. (2020). Prediction and Characterization of Therapeutic Protein Aggregation. Retrieved from https://edoc.ub.uni-muenchen.de/26123/1/Gentiluomo_Lorenzo.pdf. Accessed April 21, 2022.</mixed-citation><mixed-citation xml:lang="en">Gentiluomo, L. (2020). Prediction and Characterization of Therapeutic Protein Aggregation. Retrieved from https://edoc.ub.uni-muenchen.de/26123/1/Gentiluomo_Lorenzo.pdf. Accessed April 21, 2022.</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Falconer, R. J., Chan, C., Hughes, K., Munro, T. P. (2011). Stabilization of a monoclonal antibody during purification and formulation by addition of basic amino acid excipients. Journal of Chemical Technology and Biotechnology, 86(7), 942–948. https://doi.org/10.1002/jctb.2657</mixed-citation><mixed-citation xml:lang="en">Falconer, R. J., Chan, C., Hughes, K., Munro, T. P. (2011). Stabilization of a monoclonal antibody during purification and formulation by addition of basic amino acid excipients. Journal of Chemical Technology and Biotechnology, 86(7), 942–948. https://doi.org/10.1002/jctb.2657</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
