Catalytic Properties of Immobilized Phytase of Silvania hatchlandensis FG 3.9.1

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription Access

Abstract

A phytase preparation was obtained from the cells of haloalkalitolerant bacteria identified as Silvania hatchlandensis isolated from the soil of a soda sludge storage facility. When the enzyme was immobilized in barium alginate gel and cross-linked with activated chitosan, 97 and 95% of the native protein activity, respectively, was retained. It was shown that 70% of the phytase activity was retained when using the enzyme immobilized in alginate and bound to chitosan over 6 consecutive reaction cycles. Immobilization resulted in an insignificant decrease in the maximum reaction rate and a decrease in the Michaelis constant. Immobilized phytase was more thermally stable compared to the free form of the enzyme: the thermal inactivation constant of the immobilized enzyme at 70°C decreased by 1.1–1.2 times. The immobilized enzyme retained activity at pH 3–12; the pH optimum of the enzyme after immobilization did not change and was equal to 5.0. The specific activity of the enzyme covalently attached to activated chitosan is higher than that of the native enzyme in low and high pH environments. Immobilized phytase of haloalkalitolerant S. hatchlandensis can be used in feed production and other areas of agriculture.

Full Text

Restricted Access

About the authors

K. G. Semenova

Institute of Ecology and Genetics of Microorganisms, Ural Branch of the Russia Academy of Sciences, Perm Federal Research Center; Perm National Research Polytechnic University

Author for correspondence.
Email: yul_max@mail.ru
Russian Federation, Perm, 614081; Perm, 614990

Y. G. Maksimova

Institute of Ecology and Genetics of Microorganisms, Ural Branch of the Russia Academy of Sciences, Perm Federal Research Center; Perm State National Research University

Email: yul_max@mail.ru
Russian Federation, Perm, 614081; Perm, 614068

References

  1. Singh B., Boukhris I., Pragya, Kumar V., Yadav A., Farhat-Khemakhem A. et al. // Pedosphere. 2020. V. 30. № 3. Р. 295–313. https://doi.org/10.1016/S1002-0160(20)60010-8
  2. Jain J., Sapna, Singh B. // Process Biochem. 2016. V. 51. Р. 159–169. https://doi.org/10.1016/j.procbio.2015.12.004
  3. Balwani I., Chakravarty K., Gaur S. // Biocatal. Agric. Biotechnol. 2017. V. 12. P. 23–29. https://doi.org/10.1016/j.bcab.2017.08.010
  4. Rizwanuddin S., Kumar V., Naik B., Singh P., Mishra S., Rustagi S., Kumar V. // J. Agric. Food Res. 2023. V. 12. 100559. https://doi.org/10.1016/j.jafr.2023.100559
  5. Urgessa O.E., Koyamo R., Dinka H., Tefese K., Gemeda M.T. // Int. J. Microbiol. 2024. V. 2024. 9400374. https://doi.org/10.1155/2024/9400374
  6. Li H.-P., Han Q.-Q., Liu Q.-M., Gan Y.-N., Rensing C., Rivera W.L. et al. // Microbiol. Res. 2023. V. 272. 127375. https://doi.org/10.1016/j.micres.2023.127375
  7. Zhou Y., Anoopkumar A.N., Tarafdar A., Madhavan A., Binoop M., Lakshmi N.M. et al. // Environ. Pollut. 2022. V. 308. 119703. https://doi.org/10.1016/j.envpol.2022.119703
  8. Li C., Wang Z., Bakshi S., Pignatello J.J., Parikh S.J. // Sci. Total Environ. 2021. V. 787. 147720. https://doi.org/10.1016/j.scitotenv.2021.147720
  9. Sharma S., Gupta P., Arya S., Kaur A. // Process Biochem. 2022. V. 120. P. 22–34. https://doi.org/10.1016/j.procbio.2022.05.022
  10. Karume I. // Sustainable Chem. Environ. 2023. V. 4. 100048. https://doi.org/10.1016/j.scenv.2023.100048
  11. Mrudula Vasudevan U., Jaiswal A.K., Krishna S., Pandey A. // Bioresour. Technol. 2019. V. 278. P. 400–407. https://doi.org/10.1016/j.biortech.2019.01.065
  12. Сердюк Е.Г., Исакова Е.П., Гесслер Н.Н., Трубникова Е.В., Антипов А.Н., Дерябина Ю.И. // Прикл. биохимия и микробиология. 2019. Т. 55. № 5. С. 498–505. https://doi.org/10.1134/S055510991905012X
  13. Filippovich S.Y., Isakova E.P., Gessler N.N., Deryabina Y.I. // Bioresour. Technol. 2023. V. 379. 129030. https://doi.org/10.1016/j.biortech.2023.129030
  14. Hidayatullah M.E., Sajidan S.A., Mkumbe B.S., Greiner R. // J. Biotechnol. Biosci. 2020. V. 7. № 1. P. 105–113. https://doi.org/10.29122/jbbi.v7i1.2997
  15. Awad G., Esawy M., El-Gammal E., Ahmed H., Elnashar M., Atwa N. // Egypt. Pharm. J. 2015. V. 14. № 2. P. 87–93. https://doi.org/10.4103/1687-4315.161268
  16. Weng Y., Wan A., Li Y., Liu Y., Chen X., Song H., Zhao C.-X. // Colloids Surf. A. 2023. V. 667. 131412. https://doi.org/10.1016/j.colsurfa.2023.131412
  17. Sirin Y., Akatin M.Y., Colak A., Ertunga N.S. // Int. J. Food Prop. 2017. V. 20. № 12. P. 2911–2922. https://doi.org/10.1080/10942912.2016.1261151
  18. Yang E., Dong H., Khongkomolsakul W., Dadmohammadi Y., Abbaspourrad A. // Food Chem.: X. 2024. V. 21. 101082. https://doi.org/10.1016/j.fochx.2023.101082
  19. Handa V., Sharma D., Kaur A., Arya S.K. // Biocatal. Agric. Biotechnol. 2020. V. 25. 101600. https://doi.org/10.1016/j.bcab.2020.101600
  20. Патент РФ. 2018. № 2654595.
  21. Ахметова А.И., Мухаметзянова А.Д., Шарипова М.Р. // Ученые записки Казанского университета. 2012. Т. 54. № 2. С. 103–110.
  22. Гесслер Н.Н., Сердюк Е.Г., Исакова Е.П., Дерябина Ю.И. // Прикл. биохимия и микробиология. 2018. Т. 54. № 4. С. 347–356. https://doi.org/10.7868/S0555109918040025
  23. Шилова А.В., Максимов А.Ю., Максимова Ю.Г. // Вода и экология: проблемы и решения. 2020. № 1(81). С. 84–94. https://doi.org/10.23968/2305-3488.2020.25.1.84-94
  24. Максимова Ю.Г., Рогожникова Т.А., Овечкина Г.В., Максимов А.Ю., Демаков В.А. // Прикл. биохимия и микробиология. 2012. Т. 48. № 5. С. 484–489.
  25. Мочалова Е.М., Максимова Ю.Г. // Вестник ПГУ. Серия биология. 2020. № 1. Р. 26–32. https://doi.org/10.17072/1994-9952-2020-1-26-32
  26. Pragya, Sharma K.K., Kumar S., Manisha, Singh D., Kumar V., Singh B. // Lett. Appl. Microbiol. 2023. V. 76. № 2. ovac077. https://doi.org/10.1093/lambio/ovac077
  27. Belho K., Ambasht P.K. // J. Sci. Res. 2021. V. 65. № 1. P. 111–119. https://doi.org/10.37398/JSR.2021.650115
  28. El-Shora H.M., Khalaf S.A., El-Solia M.M. // Res. J. Pharm. Biol. Chem. Sci. 2019. V. 10. № 3. P. 529–541. https://doi.org/10.33887/rjpbcs/2019.10.3.62
  29. Dokuzparmak E., Sirin Y., Cakmak U., Ertunga N.S. // Int. J. Food Prop. 2017. V. 20. № 5. P. 1104–1116. https://doi.org/10.1080/10942912.2016.1203930

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
2. 1. Operational stability of phytase immobilized by incorporation of barium alginate (1) into the gel structure and covalent attachment to activated chitosan (2).

Download (56KB)
Indexing metadata
3. 2. The dependence of the activity of native phytase (E) on temperature.

Download (50KB)
Indexing metadata
4. 3. Thermal activation of phytase at 50 (a), 60 (b), and 70 °C (c): 1 — phytase immobilized by incorporation of barium alginate into the gel; 2 — phytase immobilized on activated chitosan; 3 — free phytase.

Download (180KB)
Indexing metadata
5. 4. Dependence of the activity of phytase immobilized in barium alginate gel (1) on activated chitosan (2) and native (3) on pH.

Download (74KB)
Indexing metadata

Copyright (c) 2025 Russian Academy of Sciences