Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene
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2015
Authors
Đokić, LidijaSpasić, Jelena
Jeremić, Sanja
Vasiljević, Branka
Prodanović, Olivera
Prodanović, Radivoje
Nikodinović-Runić, Jasmina
Article (Published version)
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The enzyme 4-oxalocrotonate tautomerase (4-OT) encoded by the xylH gene is a part of the degradation pathway of aromatic compounds in Pseudomonas putida mt-2. 4-OT was described to catalyze Michael-type addition of acetaldehyde to beta-nitrostyrene, and the whole cell system based on recombinantly expressed 4-OT has been developed previously. In this study biocatalytic process based on Escherichia coli whole cells expressing 4-OT was significantly improved using immobilization and ex situ product recovery strategies. Whole cell immobilization in alginate beads was applied in biocatalytic production of 4-nitro-3-phenyl-butanal from beta-nitrostyrene and acetaldehyde. Immobilized biocatalyst showed wider pH activity range and could tolerate twofold higher initial concentrations of substrate in comparison to the free whole cell biocatalyst. Beads retained their initial activity over 10 consecutive biotransformations of the model reaction and remained suitable for the repetitive use with 8...5 % of the initial activity after two months of storage. Bioprocess was further improved by utilizing Amberlite XAD-2 hydrophobic resin for the product recovery. With this modification, the amount of organic solvent was reduced 40-fold in comparison to previously reported method making this biocatalytic process greener.
Keywords:
Whole cell / Michael-type addition / Immobilization / Biotransformation / Alginate / 4-Oxalocrotonate tautomeraseSource:
Bioprocess and Biosystems Engineering, 2015, 38, 12, 2389-2395Publisher:
- Springer, New York
Funding / projects:
- Microbial diversity study and characterization of beneficial environmental microorganisms (RS-MESTD-Basic Research (BR or ON)-173048)
- Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-MESTD-Basic Research (BR or ON)-172049)
DOI: 10.1007/s00449-015-1474-8
ISSN: 1615-7591
PubMed: 26410191
WoS: 000363955600010
Scopus: 2-s2.0-85027945518
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Institution/Community
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Đokić, Lidija AU - Spasić, Jelena AU - Jeremić, Sanja AU - Vasiljević, Branka AU - Prodanović, Olivera AU - Prodanović, Radivoje AU - Nikodinović-Runić, Jasmina PY - 2015 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/841 AB - The enzyme 4-oxalocrotonate tautomerase (4-OT) encoded by the xylH gene is a part of the degradation pathway of aromatic compounds in Pseudomonas putida mt-2. 4-OT was described to catalyze Michael-type addition of acetaldehyde to beta-nitrostyrene, and the whole cell system based on recombinantly expressed 4-OT has been developed previously. In this study biocatalytic process based on Escherichia coli whole cells expressing 4-OT was significantly improved using immobilization and ex situ product recovery strategies. Whole cell immobilization in alginate beads was applied in biocatalytic production of 4-nitro-3-phenyl-butanal from beta-nitrostyrene and acetaldehyde. Immobilized biocatalyst showed wider pH activity range and could tolerate twofold higher initial concentrations of substrate in comparison to the free whole cell biocatalyst. Beads retained their initial activity over 10 consecutive biotransformations of the model reaction and remained suitable for the repetitive use with 85 % of the initial activity after two months of storage. Bioprocess was further improved by utilizing Amberlite XAD-2 hydrophobic resin for the product recovery. With this modification, the amount of organic solvent was reduced 40-fold in comparison to previously reported method making this biocatalytic process greener. PB - Springer, New York T2 - Bioprocess and Biosystems Engineering T1 - Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene EP - 2395 IS - 12 SP - 2389 VL - 38 DO - 10.1007/s00449-015-1474-8 ER -
@article{ author = "Đokić, Lidija and Spasić, Jelena and Jeremić, Sanja and Vasiljević, Branka and Prodanović, Olivera and Prodanović, Radivoje and Nikodinović-Runić, Jasmina", year = "2015", abstract = "The enzyme 4-oxalocrotonate tautomerase (4-OT) encoded by the xylH gene is a part of the degradation pathway of aromatic compounds in Pseudomonas putida mt-2. 4-OT was described to catalyze Michael-type addition of acetaldehyde to beta-nitrostyrene, and the whole cell system based on recombinantly expressed 4-OT has been developed previously. In this study biocatalytic process based on Escherichia coli whole cells expressing 4-OT was significantly improved using immobilization and ex situ product recovery strategies. Whole cell immobilization in alginate beads was applied in biocatalytic production of 4-nitro-3-phenyl-butanal from beta-nitrostyrene and acetaldehyde. Immobilized biocatalyst showed wider pH activity range and could tolerate twofold higher initial concentrations of substrate in comparison to the free whole cell biocatalyst. Beads retained their initial activity over 10 consecutive biotransformations of the model reaction and remained suitable for the repetitive use with 85 % of the initial activity after two months of storage. Bioprocess was further improved by utilizing Amberlite XAD-2 hydrophobic resin for the product recovery. With this modification, the amount of organic solvent was reduced 40-fold in comparison to previously reported method making this biocatalytic process greener.", publisher = "Springer, New York", journal = "Bioprocess and Biosystems Engineering", title = "Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene", pages = "2395-2389", number = "12", volume = "38", doi = "10.1007/s00449-015-1474-8" }
Đokić, L., Spasić, J., Jeremić, S., Vasiljević, B., Prodanović, O., Prodanović, R.,& Nikodinović-Runić, J.. (2015). Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene. in Bioprocess and Biosystems Engineering Springer, New York., 38(12), 2389-2395. https://doi.org/10.1007/s00449-015-1474-8
Đokić L, Spasić J, Jeremić S, Vasiljević B, Prodanović O, Prodanović R, Nikodinović-Runić J. Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene. in Bioprocess and Biosystems Engineering. 2015;38(12):2389-2395. doi:10.1007/s00449-015-1474-8 .
Đokić, Lidija, Spasić, Jelena, Jeremić, Sanja, Vasiljević, Branka, Prodanović, Olivera, Prodanović, Radivoje, Nikodinović-Runić, Jasmina, "Immobilization of Escherichia coli cells expressing 4-oxalocrotonate tautomerase for improved biotransformation of beta-nitrostyrene" in Bioprocess and Biosystems Engineering, 38, no. 12 (2015):2389-2395, https://doi.org/10.1007/s00449-015-1474-8 . .