Buy (625 RUB)
|Generate QR code
Open Access
Subscription or Fee Access
Biocatalysts Based on Bacterial Strain Cells with Amidase Activity for Synthesis of Acrylic Acid from Acrylamide
https://doi.org/10.18412/1816-0387-2019-1-73-79
Abstract
A biocatalytic process for synthesis of acrylic acid was studied in the presence of Rhodococcus erythropolis 4-1 and Alcaligenes faecalis 2 strains with the pronounced amidase activity. The optimal pH of the process was 6–7 for R. erythropolis 4-1 and 7–7.5 for A. faecalis 2, optimal temperature 20–50 °C for both strains, optimal concentration of acrylamide 150 mM for R. erythropolis 4-1 and 250 mM for A. faecalis 2. At the stepwise addition of the substrate, the synthesis was more effective with A. faecalis 2 than with R. erythropolis 4-1. Freezing at –20 °C was shown preferable for storing the biocatalysts. The amidase activity of both humid and dry stored A. faecalis 2 cells immobilized on activated glutaric aldehyde and non-activated chitosan was not decreased.
About the Authors
Yu. G. Maksimova
Institute of Ecology and Genetics of Microorganisms, Perm; Perm State University, Perm
Russian Federation
Russian Federation
M. S. Yakimova
Perm National Research Polytechnic University
Russian Federation
Russian Federation
A. Yu. Maksimov
Institute of Ecology and Genetics of Microorganisms, Perm; Perm National Research Polytechnic University; Perm State University
Russian Federation
Russian Federation
References
1. Wang X., Wang H., Sun Y. // Chem. 2017. V. 3. P. 211—228.
2. Li C., Zhu Q., Cui Z., Wang B., Fang Y., Tan T. // Chem. Eng. Sci. 2018. V. 183. P. 288—294.
3. Manzini S., Huguet N., Trapp O., Paciello R.A., Schaub T. // Catal. Today. 2017. V. 281. P. 379—386.
4. Hollering M., Dutta B., Kühn F.E. // Coord. Chem. Rev. 2016. V. 309. P. 51—67.
5. Rasteiro L.F., Vieira L.H., Possato L.G., Pulcinelli S.H., Santilli C.V., Martins L. // Catal. Today. 2017. V. 296. P. 10—18.
6. Xiaobo X.U., Jianping L.I.N., Peilin C.E.N. // Chinese J. Chem. Eng. 2006. V. 14. № 4. P. 419—427.
7. Zhang X., Lin L., Zhang T., Liu H., Zhang X. // Chem. Eng. J. 2016. V. 284. P. 934—941.
8. Shen M., Zheng Y.-G., Shen Y.-C. // Process Biochem. 2009. V. 44. P. 781—785.
9. Полтавская С.В., Козулина Т.Н., Сингирцев И.Н., Козулин С.В., Шуб Г.М., Воронин С.П. // Биотехнология. 2004. № 1. С. 62—70.
10. Пат. РФ. 2337954.
11. Максимова Ю.Г., Максимов А.Ю., Демаков В.А., Козлов С.В., Овечкина Г.В., Олонцев В.Ф. // Биотехнология. 2010. № 4. С. 51—58.
12. Максимова Ю.Г., Демаков В.А., Овечкина Г.В. // Вестник биотехнологии и физико-химической биологии имени Ю.А. Овчинникова. 2011. Т. 7. № 2. С. 5—10.
13. Справочник биохимика / Досон Р., Эллиот Д., Эллиот У., Джонс К. // М.: Мир, 1991. 544 с.
14. Joshi S.J., Abed R.M.M. // Environ. Process. 2017. V. 4. № 2. P. 463—476.
15. Zödl B., Schmid D., Wassler G., Gundacker C., Leibetseder V., Thalhammer T., Ekmekcioglu C. // Toxicology. 2007. V. 232. № 1—2. P. 99—108.
16. Ермилова Е.В. Молекулярные аспекты адаптации прокариот. СПб: Изд-во СПб. ун-та, 2007. 299 с.
17. Максимова Ю.Г., Васильев Д.М., Зорина А.С., Овечкина Г.В., Максимов А.Ю. // Прикладная биохимия и микробиология. 2018. Т. 54. № 2. С. 158—164.
18. Thakur N., Kumar V., Sharma N.K., Thakur S., Bhalla T.C. // Protein Pept Lett. 2016. V. 23. № 2. P. 152—158.
19. Глинский С.А., Козулин С.В., Козулина Т.Н., Полтавская С.В., Яненко А.С., Леонова Т.Е. // Биотехнология. 2010. № 1. С. 17—24.
Review
For citations:
Maksimova Yu.G., Yakimova M.S., Maksimov A.Yu. Biocatalysts Based on Bacterial Strain Cells with Amidase Activity for Synthesis of Acrylic Acid from Acrylamide. Kataliz v promyshlennosti. 2019;19(1):73-79. (In Russ.) https://doi.org/10.18412/1816-0387-2019-1-73-79
Views:
640
Email this article 