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<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="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">vestib</journal-id><journal-title-group><journal-title xml:lang="ru">Известия Национальной  академии наук Беларуси. Серия биологических наук</journal-title><trans-title-group xml:lang="en"><trans-title>Proceedings of the National Academy of Sciences of Belarus, Biological Series</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1029-8940</issn><issn pub-type="epub">2524-230X</issn><publisher><publisher-name>The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.29235/1029-8940-2022-67-3-274-284</article-id><article-id custom-type="elpub" pub-id-type="custom">vestib-820</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>Молекулярно-генетический анализ детерминант, кодирующих β-галактозидазы бактерий</article-title><trans-title-group xml:lang="en"><trans-title>Мolecular-genetic analysis of determinants encoding β-galactosidases of bacteria Bifidobacterium longum BIM B-813 D</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Морозова</surname><given-names>А. Н.</given-names></name><name name-style="western" xml:lang="en"><surname>Morozova</surname><given-names>A. N.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Морозова Антонина Николаевна – науч. сотрудник</p><p>ул. Купревича, 2, 220141, г. Минск</p></bio><bio xml:lang="en"><p>Antonina N. Morozova – Researcher</p><p>2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">bifidoby@yandex.by</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Охремчук</surname><given-names>А. Э.</given-names></name><name name-style="western" xml:lang="en"><surname>Akhremchuk</surname><given-names>A. E.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Охремчук Артур Эдуардович – мл. науч. сотрудник</p><p>ул. Купревича, 2, 220141, г. Минск</p></bio><bio xml:lang="en"><p>Artur E. Akhremchuk – Junior Researcher</p><p>2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">okhrem4ukartur@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Головнева</surname><given-names>Н. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Golovnyova</surname><given-names>N. А.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Головнева Наталья Алексеевна – канд. биол. наук, заведующий лабораторией</p><p>ул. Купревича, 2, 220141, г. Минск</p></bio><bio xml:lang="en"><p>Natalia A. Golovnyova – Ph. D. (Biol.), Head of the Labo­ ratory</p><p>2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">bifidoby@yandex.by</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Институт микробиологии НАН Беларуси</institution></aff><aff xml:lang="en"><institution>Institute of Microbiology of the National Academy of Sciences of Belarus</institution></aff></aff-alternatives><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>02</day><month>08</month><year>2022</year></pub-date><volume>67</volume><issue>3</issue><fpage>274</fpage><lpage>284</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Морозова А.Н., Охремчук А.Э., Головнева Н.А., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Морозова А.Н., Охремчук А.Э., Головнева Н.А.</copyright-holder><copyright-holder xml:lang="en">Morozova A.N., Akhremchuk A.E., Golovnyova N.А.</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://vestibio.belnauka.by/jour/article/view/820">https://vestibio.belnauka.by/jour/article/view/820</self-uri><abstract><p>Проведен молекулярно-генетический анализ генома бактерий B. longum БИМ B-813Д, отличающихся высоким уровнем продукции β-галактозидазы. В геноме B. longum БИМ B-813Д выявлены гены Bgal_small_N, lacZ1, bgaB1, bgaB2, bgaB3 и lacZ2, кодирующие синтез β-галактозидаз. Предполагается, что lacZ1, bgaB2 и bgaB3, характеризующиеся высокой степенью идентичности с генами близкородственных видов бифидобактерий, кодируют ферменты, которые осуществляют специфические реакции гидролиза и трансгликозилирования углеводов. Установлено, что ферменты BgaB1, BgaB2 и BgaB3 относятся к семейству GH42 гликозил-гидролаз, а LacZ1 и LacZ2 – к семейству GH2. Детально рассмотрены области генома, кодирующие синтез β-галактозидаз В. longum БИМ В-813 Д. Сравнительный анализ локуса lacZ1 B. longum БИМ B-813 Д и сходной области генома AS143_01230 B. longum subsp. longum MC-42 показал наличие у B. longum БИМ B-813 гена транспозазы ISL3. Предполагается, что наличие инсерционной последовательности ISL3 в области lacZ1 приводит к изменению экспрессии гена и увеличению продукции β-галактозидазы у B. longum БИМ B-813Д.</p></abstract><trans-abstract xml:lang="en"><p>The molecular-genetic analysis of the bacterial genome of the strain B. longum BIM B-813D distinguished by a high level of β-galactosidase production was performed. Genes Bgal_small_N, lacZ1, bgaB1, bgaB2 and bgaB3, and lacZ2, encoding the synthesis of β-galactosidases, were revealed in the deciphered genome. It was shown that the genes lacZ1, bgaB2, and bgaB3 characterized by an enhanced degree of similarity to the genes of closely related bifidobacterial species, presumably code for the enzymes catalyzing the specific reactions of hydrolysis and transglycosylation of carbohydrates. It was found that the enzymes BgaB1, BgaB2 and BgaB3 belong to the GH42 family of glycosyl hydrolases, whereas the enzymes LacZ1 and LacZ2 – to the GH2 family. The genome domains responsible for the synthesis of β-galactosidases in the strain B. longum BIM B-813D were studied in detail. A comparative analysis of the locus of lacZ1 in B. longum BIM B-813D and the similar genome fragment AS143_01230 from B. longum subsp. longum MC-42 detected the presence of the transposase gene ISL3 in the former strain. It was suggested that the insertion of the sequence of ISL3 in the lacZ1 locus resulted in the modified gene expression and the increased production of β-galactosidase in the strain B. longum BIM B-813D.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>бифидобактерии</kwd><kwd>гликозил-гидролазы</kwd><kwd>Bifidobacterium longum</kwd><kwd>β-галактозидаза</kwd><kwd>гидролиз лактозы</kwd><kwd>трансгликозилирование</kwd></kwd-group><kwd-group xml:lang="en"><kwd>bifidobacteria</kwd><kwd>glycosyl hydrolases</kwd><kwd>Bifidobacterium longum</kwd><kwd>β-galactosidases</kwd><kwd>lactose hydrolysis</kwd><kwd>transglycosylation</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Микробиота / под ред. Е. Л. Никонова, Е. Н. Поповой. ‒ М. : Медиа Сфера, 2019. ‒ 256 с.</mixed-citation><mixed-citation xml:lang="en">Nikonova E. L., Popova E. N. (eds.). Mikrobiota. Moscow, Media Sfera Publ., 2019. 256 p. (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Mitsuoka, T. Development of functional foods / T. Mitsuoka // Biosci. Microbiota Food Health. – 2014. – Vol. 33, N 3. – P. 117‒128. https://doi.org/10.12938/bmfh.33.117</mixed-citation><mixed-citation xml:lang="en">Mitsuoka T. Development of functional foods. Bioscience of Microbiota, Food and Health, 2014, vol. 33, no. 3, pp. 117‒128. https://doi.org/10.12938/bmfh.33.117</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Rodriguez, C. I. Evolutionary relationships among bifidobacteria and their hosts and environments / C. I. Rodriguez, J. B. H. Martiny // BMC Genomics. – 2020. – Vol. 21, N 1. ‒ Art. 26. https://doi.org/10.1186/s12864-019-6435-1</mixed-citation><mixed-citation xml:lang="en">Rodriguez C. I., Martiny J. B. H. Evolutionary relationships among bifidobacteria and their hosts and environments. BMC Genomics, 2020, vol. 21, no. 1, art. 26. https://doi.org/10.1186/s12864-019-6435-1</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Klijn, A. Lessons from the genomes of bifidobacteria / A. Klijn, A. Mercenier, F. Arigoni // FEMS Microbiol. Rev. – 2005. – Vol. 29, N 3. – P. 491‒509. https://doi.org/10.1016/j.femsre.2005.04.010</mixed-citation><mixed-citation xml:lang="en">Klijn A., Mercenier A., Arigoni F. Lessons from the genomes of bifidobacteria. FEMS Microbiology Reviews, 2005, vol. 29, no. 3, pp. 491‒509. https://doi.org/10.1016/j.femsre.2005.04.010</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Pokusaeva, K. Carbohydrate metabolism in Bifidobacteria / K. Pokusaeva, G. F. Fitzgerald, D. van Sinderen // Genes Nutr. – 2011. – Vol. 6, N 3. – P. 285‒306. https://doi.org/10.1007/s12263-010-0206-6</mixed-citation><mixed-citation xml:lang="en">Pokusaeva K., Fitzgerald D., van Sinderen G. F. Carbohydrate metabolism in Bifidobacteria. Genes and Nutrition, 2011, vol. 6, no. 3, pp. 285‒306. https://doi.org/10.1007/s12263-010-0206-6</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Uchil, P. D. β-Galactosidase / P. D. Uchil, A. Nagarajan, P. Kumar // Cold Spring Harb. Protoc. – 2017. – Vol. 2017, N 10. https://doi.org/10.1101/pdb.top096198</mixed-citation><mixed-citation xml:lang="en">Uchil P. D., Nagarajan A., Kumar P. β-Galactosidase. Cold Spring Harbor Protocols, 2017, vol. 2017, no. 10. https://doi.org/10.1101/pdb.top096198</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Zolnere, K. The comparison of commercially available β-galactosidases for dairy industry: review / K. Zolnere, Ciprovica // The Annual 23th International scientific conference “Research for Rural Development 2017” (Jelgava (Latvia), May 17–19, 2017) / Latvia Univ. of Agriculture. – Jelgava, 2017. – Vol. 1. – P. 215–222.</mixed-citation><mixed-citation xml:lang="en">Zolnere K. Ciprovica I. The comparison of commercially available β-galactosidases for dairy industry: review. The Annual 23th International scientific conference “Research for Rural Development 2017” (Jelgava (Latvia), May 17–19, 2017). Vol. 1. Jelgava, 2017, pp. 215–222.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Transgalactosylation and hydrolytic activities of commercial preparations of β-galactosidase for the synthesis of prebiotic carbohydrates / C. Guerrero [et al.] // Enzyme Microb. Technol. – 2015. – Vol. 70. – P. 9‒17. https://doi.org/10.1016/j.enzmictec.2014.12.006</mixed-citation><mixed-citation xml:lang="en">Guerrero C., Vera C., Conejeros R., Illanes A. Transgalactosylation and hydrolytic activities of commercial preparations of β-galactosidase for the synthesis of prebiotic carbohydrates. Enzyme and Microbial Technology, 2015, vol. 70, pp. 9‒17. https://doi.org/10.1016/j.enzmictec.2014.12.006</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Морозова, А. Н. Использование химического мутагенеза для получения штамма бифидобактерий с повышенной продукцией β-галактозидазы / А. Н. Морозова, Н. А. Головнева // Молодежь в науке ‒ 2011 : материалы Междунар. науч. конф. молодых ученых, г. Минск, 25‒29 апр. 2011 г. : в 5 ч. ‒ Минск, 2012. ‒ Ч. 3 : Сер. биол. наук ; Сер. мед. наук / редкол. : И. Д. Волотовский (гл. ред.) [и др.]. ‒ С. 132–135.</mixed-citation><mixed-citation xml:lang="en">Morozova A. N., Golovneva N. A. The use of chemical mutagenesis to generate a strain of bifidobacteria with increased production of β-galactosidase. Molodezh’ v nauke ‒ 2011: materialy Mezhdunarodnoi nauchnoi konferentsii molodykh uchenykh (g. Minsk, 25‒29 aprelya 2011 goda). Chast’ 3: Seriya biologicheskikh nauk; Seriya meditsinskikh nauk [Youth in Science – 2011: Proceedings of the International scientific conference of young scientists (Minsk, April 25–29, 2011). Part 3: Biological sciences series; Medical sciences series]. Minsk, 2011, pp. 132–135 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Морозова, А. Н. Особенности генома Bifidobacterium longum БИМ B-813Д, отражающие адаптацию бактерий к среде обитания / А. Н. Морозова, А. Э. Охремчук, Н. А. Головнева // Микробные биотехнологии: фундаментальные и прикладные аспекты : сб. науч. тр. / редкол. : Э. И. Коломиец [и др.]. – Минск, 2021. – Т. 13. – С. 66‒76.</mixed-citation><mixed-citation xml:lang="en">Morozova A. N., Okhremchuk A. E., Golovneva N. A. Genome characteristics of Bifidobacterium longum BIM B­813D, reflecting the ability of bacteria to adapt to the environment. Mikrobnye biotekhnologii: fundamental’nye i prikladnye aspekty: sbornik nauchnykh trudov. Tom 13 [Microbial biotechnologies: fundamental and applied aspects: collection of sci­ entific works. Volume 13]. Minsk, 2021, pp. 66‒76 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Tupikin, A. E. Draft genome sequence of the probiotic Bifidobacterium longum subsp. longum strain MC-42 / A. E. Tupikin, A. I. Kalmykova, M. Kabilov // Genome Announc. – 2016. – Vol. 4, N 6. – P. e01411-16. https://doi.org/10.1128/genomeA.01411-16</mixed-citation><mixed-citation xml:lang="en">Tupikin A. E., Kalmykova A. I., Kabilov M. Draft genome sequence of the probiotic Bifidobacterium longum subsp. longum strain MC­42. Genome Announcements, 2016, vol. 4, no. 6, pp. e01411­16. https://doi.org/10.1128/genomeA.01411­16</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Devika, N. T. Deciphering the metabolic capabilities of Bifidobacteria using genome-scale metabolic models / N. T. Devika, K. Raman // Sci. Rep. – 2019. – Vol. 9, N 1. – Art. 18222. https://doi.org/10.1038/s41598-019-54696-9</mixed-citation><mixed-citation xml:lang="en">Devika N. T., Raman K. Deciphering the metabolic capabilities of Bifidobacteria using genome­scale metabolic models. Scientific Reports, 2019, vol. 9, no. 1, art. 18222. https://doi.org/10.1038/s41598­019­54696­9</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">The abundance and variety of carbohydrate-active enzymes in the human gut microbiota / A. E. Kaoutari [et al.] // Nat. Rev. Microbiol. – 2013. – Vol. 11, N 7. – P. 497‒504. https://doi.org/10.1038/nrmicro3050</mixed-citation><mixed-citation xml:lang="en">Kaoutari A., Armougom F., Gordon J. I., Raoult D., Henrissat B. The abundance and variety of carbohydrate­active enzymes in the human gut microbiota. Nature Reviews Microbiology, 2013, vol. 11, no. 7, pp. 497‒504. https://doi.org/10.1038/nrmicro3050</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">A structural view of the action of Escherichia coli (lacZ), β-galactosidase / D. H. Juers [et al.] // Biochemistry. – 2001. – Vol. 40, N 49. – P. 14781‒14794. https://doi.org/10.1021/bi011727i</mixed-citation><mixed-citation xml:lang="en">Juers D. H., Heightman T. D., Vasella A., McCarter J. D., Mackenzie L., Withers S. G., Matthews B. W. A Structural view of the action of Escherichia coli (lacZ)‚ β­galactosidase. Biochemistry, 2001, vol. 40, no. 49, pp. 14781‒14794. https://doi.org/10.1021/bi011727i</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">α-Amylase: an enzyme specificity found in various familiesof glycoside hydrolases / Š. Janeček [et al.] // Cell. Mol. Life Sci. – 2014. – Vol. 71, N 7. – P. 1149–1170. https://doi.org/10.1007/s00018-013-1388-z</mixed-citation><mixed-citation xml:lang="en">Janeček Š., Svensson B., MacGregor E. A. α­Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cellular and Molecular Life Sciences, 2014, vol. 71, no. 7, pp. 1149‒1170. https://doi.org/10.1007/s00018­013­1388­z</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Galactosidases of strain Bifidobacterium Longum Bim В-813d with transglycosylating activity / A. Morozova [et al.] // Eurasian J. Appl. Biotechnol. – 2021. – N 2. https://doi.org/10.11134/btp.2.2021.5</mixed-citation><mixed-citation xml:lang="en">Morozova A., Golovnyova N., Ryabaya N., Safonova M. Galactosidases of strain Bifidobacterium Longum Bim В­813d with transglycosylating activity. Eurasian Journal of Applied Biotechnology, 2021, no. 2. https://doi.org/10.11134/btp.2.2021.5</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Guglielmetti1, S. Mobilome and genetic modification of bifidobacteria / S. Guglielmetti1, B. Mayo, P. Álvarez-Martín // Beneficial Microbes. – 2013. – Vol. 4, N 2. – P. 143‒166. https://doi.org/10.3920/BM2012.0031</mixed-citation><mixed-citation xml:lang="en">Guglielmetti1 S., Mayo B., Álvarez­Martín P. Mobilome and genetic modification of bifidobacteria. Beneficial Microbes, 2013, vol. 4, no. 2, pp. 143‒166. https://doi.org/10.3920/BM2012.0031</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Structural explanation for allolactose (lac operon inducer) synthesis by lacZ β-galactosidase and the evolutionary relationship between allolactose synthesis and the lac repressor / R. W. Wheatley [et al.] // J. Biol. Chem. – 2013. – Vol. 288, N 18. – P. 12993‒3005. https://doi.org/10.1074/jbc.M113.455436</mixed-citation><mixed-citation xml:lang="en">Wheatley R. W., Lo S., Jancewicz L. J., Dugdale M. L., Huber R. E. Structural explanation for allolactose (lac operon inducer) synthesis by lacZ β­galactosidase and the evolutionary relationship between allolactose synthesis and the lac repressor. Journal of Biological Chemistry, 2013, vol. 288, no. 18, pp. 12993‒3005. https://doi.org/10.1074/jbc.M113.455436</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Zafar, H. Comparative analyses of the transport proteins encoded within the genomes of nine bifidobacterium species / Н. Zafar, M. H. Saier (Jr.) // Microb. Physiol. – 2022. – Vol. 32, N 1–2. – P. 30‒44. https://doi.org/10.1159/000518954</mixed-citation><mixed-citation xml:lang="en">Zafar H., Saier M. H. (Jr.) Comparative analyses of the transport proteins encoded within the genomes of nine bifidobacterium species. Microbial Physiology, 2022, vol. 32, no. 1–2, pp. 30‒44. https://doi.org/10.1159/000518954</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Cloning and characterization of a mammalian proton-coupled metal-ion transporter / H. Gunshin [et al.] // Nature. – 1997. – Vol. 388, N 6641. – P. 482‒488. https://doi.org/10.1038/41343</mixed-citation><mixed-citation xml:lang="en">Gunshin H., Mackenzie B., Berger U. V., Gunshin Y., Romero M. F., Boron W. F., Nussberger S., Gollan J. L., Hedi­ ger M. A. Cloning and characterization of a mammalian proton­coupled metal­ion transporter. Nature, 1997, vol. 388, no. 6641, pp. 482–488. https://doi.org/10.1038/41343</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Comparative genomics and evolution of regulons of the LacI-family transcription factors / D. A. Ravcheev [et al.] // Front. Microbiol. – 2014. – Vol. 5. – Art. 294. https://doi.org/10.3389/fmicb.2014.00294</mixed-citation><mixed-citation xml:lang="en">Ravcheev D. A., Khoroshkin M. S., Laikova O. N., Tsoy O. V., Sernova N. V., Petrova S. A., Rakhmaninova A. B., Novichkov P. S., Gelfand M. S., Rodiono D. A. Comparative genomics and evolution of regulons of the LacI­family transcription factors. Frontiers in Microbiology, 2014, vol. 5, art. 294. https://doi.org/10.3389/fmicb.2014.00294</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Genomics of the genus bifidobacterium reveals species-specific adaptation to the glycan-rich gut environment / C. Milani [et al.] // Appl. Environ. Microbiol. – 2016. – Vol. 82, N 4. – P. 980‒991. https://doi.org/10.1128/AEM.03500-15</mixed-citation><mixed-citation xml:lang="en">Milani Ch., Turroni F., Duranti S., Lugli G. A., Mancabelli L., Ferrario Ch., Sinderen D., Ventura M. Genomics of the genus Bifidobacterium reveals species­specific adaptation to the glycan­rich gut environment. Applied and Environmental Microbiology, 2016, vol. 82, no. 4, pp. 980‒991. https://doi.org/10.1128/AEM.03500­15</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>
