The Obtaining of Recombinant Producer of Trametes hirsuta Versatile Peroxidase VP2 in Penicillium canescens

Мұқаба

Дәйексөз келтіру

Толық мәтін

Ашық рұқсат Ашық рұқсат
Рұқсат жабық Рұқсат берілді
Рұқсат жабық Рұқсат ақылы немесе тек жазылушылар үшін

Аннотация

The interest in peroxidases of the basidiomycetes secreted enzyme complex is due to their wide substrate specificity and the ability of these enzymes to participate in the biodegradation of such difficultly degradable biopolymers as lignin. However, due to the difficulty of isolating these enzymes from native sources, their study is difficult. In this work, expression vectors were created that carried the sequence encoding the T. hirsuta LE-BIN072 versatile peroxidase VP2, which was transformed into the genome of the P. canescens strain. Screening of transformants showed the presence of peroxidase activity up to 1 U/mL. Fragments of the target protein in the culture liquid of the selected transformants were identified by mass spectrometric analysis. A new strain of P. canescens pVP2D-6, a producer of the recombinant universal peroxidase VP2 T. hirsuta LE-BIN072, was obtained for the first time, and the ability of the enzyme complex secreted by it to modify alkaline lignin was shown.

Авторлар туралы

O. Savinova

Bach Institute of Biochemistry, Biotechnology Research Center of Russian Academy of Sciences

Хат алмасуға жауапты Автор.
Email: savinova_os@rambler.ru
Russia, 119071, Moscow

A. Chulkin

Bach Institute of Biochemistry, Biotechnology Research Center of Russian Academy of Sciences

Email: savinova_os@rambler.ru
Russia, 119071, Moscow

K. Moiseenko

Bach Institute of Biochemistry, Biotechnology Research Center of Russian Academy of Sciences

Email: savinova_os@rambler.ru
Russia, 119071, Moscow

T. Fedorova

Bach Institute of Biochemistry, Biotechnology Research Center of Russian Academy of Sciences

Email: savinova_os@rambler.ru
Russia, 119071, Moscow

Әдебиет тізімі

  1. Ponnusamy V.K., Nguyen D.D., Dharmaraja J., Shobana S., Banu J.R., Saratale R.G. et al. // Bioresour. Technol. 2019. V. 271. P. 462–472. https://doi.org/10.1016/j.biortech.2018.09.070
  2. Biko O. D.V., Viljoen-Bloom M., van Zyl W. H. // Enzyme Microb. 2021. V. 141, 109669. https://doi.org/10.1016/j.enzmictec.2020.109669
  3. Kainthola J., Podder A., Fechner M., Goel R. // Bioresour. Technol. 2021. V. 321. 124397. https://doi.org/10.1016/j.biortech.2020.124397
  4. Abbas A., Koc H., Liu F., Tien M. // Curr Genet. 2005. V. 47. P. 49–56. https://doi.org/10.1007/s00294-004-0550-4
  5. Dashtban M., Schraft H., Syed T.A., Qin W. // Int. J. Biochem. Mol. Biol. 2010. V. 1. P. 36–50.
  6. Zhang S., Xiao J., Wanga G., Chen G. // Bioresour. Technol. 2020. V. 304. 122975. https://doi.org/10.1016/j.biortech.2020.122975
  7. Liers C., Aranda E., Strittmatter E., Piontek K., Plattner D.A., Zorn H. et al. // J. Mol. Catal. B Enzym. 2014. V. 103. P. 41–46. https://doi.org/10.1016/j.molcatb.2013.09.025
  8. Moiseenko K.V., Glazunova O.A., Savinova O.S., Vasina D.V., Zherebker A.Ya., Kulikova N.A. et al. // Bioresour. Technol. 2021. V. 335. 125229. https://doi.org/10.1016/j.biortech.2021.125229
  9. Vasina D.V., Moiseenko K.V., Fedorova T.V., Tyazhelova T.V. // PLoS ONE. 2017. V. 12. № 3. e0173813. https://doi.org/10.1371/journal.pone.0173813
  10. Savinova O.S., Shabaev A.V., Glazunova O.A., Moiseenko K.V., Fedorova T.V. // Appl. Biochem. Microbiol. 2022. V. 58. Suppl. 1. P. S113–S125.
  11. Fernández-Fueyo E., Ruiz-Dueñas F.J., Martínez M.J., Romero A., Hammel K.E., Medrano F.J., Martínez A.T. // Biotechnol. Biofuels. 2014. V. 7. № 2. https://doi.org/10.1186/1754-6834-7-2
  12. Ruiz-Duenas F.J., Morales M., Garcia E., Miki Y., Martinez M.J., Martinez A.T. // J. Exp. Bot. 2009. V. 60. № 2. P. 441–452. https://doi.org/10.1093/jxb/ern261
  13. Rodakiewicz-Nowak J., Jarosz-Wilkolazka A., Luterek J. // Applied Catalysis A: General. 2006. V. 308. P. 56–61.
  14. Perez-Boada M., Doyle W.A., Ruiz-Duenas F.J., Martinez M.J., Martinez A.T. // Enzyme Microb. Technol. 2002. V. 30. P. 518–524.
  15. Majekea B.M., García-Aparicioa M., Biko O.D, Viljoen-Bloom M., van Zyl W.H., Görgensa J.F. // Enzyme Microb. 2020. V. 139. 109593.https://doi.org/10.1016/j.enzmictec.2020.109593
  16. Stewart P., Whitwam R. E., Kersten P. J., Cullen D., Tien M. // Appl. Environ. Microbiol. 1996. V. 62. № 3. P. 860–864. https://doi.org/10.1128/aem.62.3.860-864.1996
  17. Sugano Y., Nakano R., Sasaki K., Shoda M. // Physiology and Biotechnology. 2000. V. 66. № 4. https://doi.org/10.1128/AEM.66.4.1754-1758.2000
  18. Chekushina A.V., Dotsenko G.S., Sinitsyn A.P. // Catalysis in Industry. 2013. V. 5 № 1. P. 98–104. https://doi.org/10.1134/S2070050413010042
  19. Savinova O.S., Moiseenko K.V., Vavilova E.A., Tyazhelova T.V., Vasina D.V. // Biochimie. 2017. V. 142. P. 183–190. https://doi.org/10.1016/j.biochi.2017.09.013
  20. Savinova O.S., Moiseenko K.V., Vavilova E.A., Chulkin A.M., Fedorova T.V., Tyazhelova T.V., Vasina D.V. // Front. Microbiol. 2019. V. 10. 152. https://doi.org/10.3389/fmicb.2019.00152
  21. Abyanova A.R., Chulkin A.M., Vavilova E.A., Fedorova T.V., Loginov D.S., Koroleva O.V., Benevolensky S.V. // Appl. Biochem. Microbiol. 2010. V. 46. № 3. P. 313–317.
  22. Aleksenko A.Y., Makarova N.A., Nikolaev I.V., Clutterbuck A.J. // Curr. Genet. 1995. V. 28. P. 474–478.
  23. Чулкин А.М., Логинов Д.С., Вавилова Е.А., Абянова А.Р., Зоров И.Н., Курзеев С.А., Королева О.В., Беневоленский С.В. // Прикл. биохимия и микробиология. 2009. Т. 45. № 2. С. 163–170.
  24. Fraczek M.G., Zhao C., Dineen L., Lebedinec R., Bowyer P., Bromley D., Delneri M. Current Protocols in Microbiology. 2019. V. 54. e89. https://doi.org/10.1002/cpmc.89
  25. Unkles S.E., Campbell E.I., Punt P.J., Hawker K.L., Contreras R., Hawkins A.R. et al. // Gene. 1992. V. 111. № 2. P. 149–155.
  26. Shabaev A.V., Moiseenko K.V., Glazunova O.A., Savinova O.S., Fedorova T.V. // Int. J. Mol. Sci. 2022. V. 23. № 10322. https://doi.org/10.3390/ ijms231810322
  27. Лисов А.В., Заварзина А.Г., Белова О.В., Леонтьевский А.А. // Микробиология. 2020. Т. 89. № 3. С. 300–307. https://doi.org/10.31857/S0026365620030118
  28. Sinitsyn A.P., Rozhkova A.M. Microorganisms in Biorefineries. Penicillium canescens Host as the Platform for Development of a New Recombinant Strain Producers of Carbohydrases. / Ed. B. Kamm Berlin, Heidelberg: Springer-Verlag, 2015. V. 26. P. 1–19.
  29. Королева О.В., Федорова Т.В., Беневоленский С.В., Вавилова Е.А., Чулкин А.М. // Патент РФ. 2015. № 2538149.
  30. Айзенштадт М.А., Боголицын К.Г. // Химия растительного сырья. 2009. № 2. С. 5–18.
  31. Ruwoldt J., Tanase-Opedal M., Syverud K. // ACS Omega. 2022. V. 7. P. 46371–46383.https://doi.org/10.1021/acsomega.2c04982
  32. Sadeghifar H., Ragauskas A. // Polymers. 2020. V. 12. № 5. P. 1134. https://doi.org/10.3390/polym12051134
  33. Lara M.A., Rodriguez-Malaver A.J., Rojas O.J., Holmquist O., Gonzalez A.M., Bullon J., Penaloza N., Araujo E. // International Biodeterioration & Biodegradation. 2003. V. 52. P. 167–173. https://doi.org/10.1016/S0964-8305(03)00055-6
  34. Amara S., Perrot T., Navarro D., Deroy A., Benkhelfallah A., Chalak A. et al. // Appl. Environ. Microbiol. 2018. V. 84. e02826-17. https://doi.org/10.1128/AEM.02826-17
  35. Sáez-Jiménez V., Rencoret J., Rodríguez-Carvajal M.A., Gutiérrez A., Ruiz-Dueñas F.J., Martínez A.T. // Biotechnol Biofuels. 2016. V. 9. P. 198. doi.org/https://doi.org/10.1186/s13068-016-0615-x
  36. Silva D., Sousa A.C., Robalo M.P., Martins L.O. // New Biotechnology. 2022. https://doi.org/10.1016/j.nbt.2022.12.003
  37. Moiseenko K.V., Glazunova O.A., Savinova O.S., Vasina D.V., Zherebker A.Ya., Kulikova N.A., Nikolaev E.N., Fedorova T.V. // Bioresour. Technol. 2021. V. 335. 125229. https://doi.org/10.1016/j.biortech.2021.125229

Қосымша файлдар


© О.С. Савинова, А.М. Чулкин, К.В. Моисеенко, Т.В. Федорова, 2023