One-Pot Biosynthesis of 3-Aminopropionic Acid from Fumaric Acid Using Recombinant Bacillus megaterium Containing a Linear Dual-Enzyme Cascade.
3-Aminopropionic acid
Aspartate ammonia-lyase
Aspartate-1-decarboxylase
Bacillus megaterium
Dual-enzyme cascade
Fumaric acid
Journal
Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561
Informations de publication
Date de publication:
Apr 2022
Apr 2022
Historique:
accepted:
30
11
2021
pubmed:
9
1
2022
medline:
16
4
2022
entrez:
8
1
2022
Statut:
ppublish
Résumé
3-Aminopropionic acid (3-APA) has wide applications in food, cosmetics, pharmaceuticals, chemical, and polymer industries. This present study aimed to develop an eco-friendly whole-cell biocatalytic process for the bio-production of 3-APA from fumaric acid (FA) using Bacillus megaterium. A dual-enzyme cascade route with aspartate-1-decarboxylases (ADC) from Bacillus subtilis and native aspartate ammonia-lyase (AspA) was developed. Divergent catalytic efficiencies between these two enzymes led to an imbalance between both enzyme reactions. In order to coordinate AspA and ADC expression levels, gene mining, optimization, and duplication strategies were employed. Additionally, culture cultivation conditions and biocatalysis process parameters were optimized. A maximum 3-APA titer was obtained (11.68 ± 0.26 g/L) with a yield of 0.78 g/g under the following optimal conditions: 45 °C, pH 6.0, and 15 g/L FA. This study established a biocatalysis process for the production of 3-APA from FA using the whole cells of the recombinant B. megaterium.
Identifiants
pubmed: 34997447
doi: 10.1007/s12010-021-03783-7
pii: 10.1007/s12010-021-03783-7
doi:
Substances chimiques
Fumarates
0
beta-Alanine
11P2JDE17B
fumaric acid
88XHZ13131
Aspartate Ammonia-Lyase
EC 4.3.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1740-1754Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Srinivasamurthy, V. S., Böttcher, D., & Bornscheuer, U. T. (2019). A multi-enzyme cascade reaction for the production of 6-hydroxyhexanoic acid. Zeitschrift für Naturforschung C, 74, 71–76.
Hold, C., Billerbeck, S., & Panke, S. (2016). Forward design of a complex enzyme cascade reaction. Nature Communications, 7, 1–8.
Sperl, J. M., & Sieber, V. (2018). (2018) Multienzyme cascade reactions -Status and recent advances. ACS Catalysis, 8, 2385–2396.
Liu, J., Tian, K., & Li, Z. (2020). in Biomass. In A. Pandey, S. V. Mohan, J.-S. Chang, P. Hallenbeck, & C. Larroche (Eds.), Biofuels, Biochemicals (pp. 427–447). Elsevier.
Peters, C., & Buller, R. (2019). Linear enzyme cascade for the production of (–)-iso-isopulegol. Zeitschrift für Naturforschung C, 74, 63–70.
Abidin, M. Z., Saravanan, T., Zhang, J., Tepper, P. G., Strauss, E., & Poelarends, G. J. (2018). Modular enzymatic cascade synthesis of vitamin B
Qian, Y., Liu, J., Song, W., Chen, X., Luo, Q., & Liu, L. (2018). Production of β-alanine from fumaric acid using a dual-enzyme cascade. ChemCatChem, 10, 4984–4991.
Enoki, J., Meisborn, J., Müller, A.-C., & Kourist, R. (2016). A multi-enzymatic cascade reaction for the stereoselective production of γ-oxyfunctionalyzed amino acids. Frontiers in Microbiology, 7, 425.
Könst, P. M., Franssen, M. C., Scott, E. L., & Sanders, J. P. (2009). A study on the applicability of L-aspartate α-decarboxylase in the biobased production of nitrogen containing chemicals. Green Chemistry, 11, 1646–1652.
Song, C. W., Lee, J., Ko, Y.-S., & Lee, S. Y. (2015). Metabolic engineering of Escherichia coli for the production of 3-aminopropionic acid. Metabolic Engineering, 30, 121–129.
Shen, Y., Zhao, L., Li, Y., Zhang, L., & Shi, G. (2014). Synthesis of β-alanine from L-aspartate using L-aspartate-α-decarboxylase from Corynebacterium glutamicum. Biotechnology Letters, 36, 1681–1686.
Pei, W., Zhang, J., Deng, S., Tigu, F., Li, Y., Li, Q., Cai, Z., & Li, Y. (2017). Molecular engineering of L-aspartate-α-decarboxylase for improved activity and catalytic stability. Applied Microbiology and Biotechnology, 101, 6015–6021.
Zou, X., Guo, L., Huang, L., Li, M., Zhang, S., Yang, A., Zhang, Y., Zhu, L., Zhang, H., & Zhang, J. (2020). Pathway construction and metabolic engineering for fermentative production of β-alanine in Escherichia coli. Applied Microbiology and Biotechnology, 104, 2545–2559.
Zhang, T., Zhang, R., Xu, M., Zhang, X., Yang, T., Liu, F., Yang, S., & Rao, Z. (2018). Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate α-decarboxylase for an efficient β-alanine production. Process Biochemistry, 70, 117–123.
Li, H., Lu, X., Chen, K., Yang, J., Zhang, A., Wang, X., & Ouyang, P. (2018). β-Alanine production using whole-cell biocatalysts in recombinant Escherichia coli. Molecular Catalysis, 449, 93–98.
Qian, Y., Lu, C., Liu, J., Song, W., Chen, X., Luo, Q., Liu, L., & Wu, J. (2020). Engineering protonation conformation of l-aspartate-α-decarboxylase to relieve mechanism-based inactivation. Biotechnology and Bioengineering, 117, 1607–1614.
Bunk, B., Schulz, A., Stammen, S., Münch, R., Warren, M. J., Jahn, D., & Biedendieck, R. (2010). A short story about a big magic bug. Bioengineered Bugs, 1, 85–91.
Biedendieck, R. (2016) A Bacillus megaterium system for the production of recombinant proteins and protein complexes. Advanced Technologies for Protein Complex Production and Characterization, 97–113.
Nehru, G., Tadi, S. R. R., Limaye, A. M., & Sivaprakasam, S. (2020). Production and characterization of low molecular weight heparosan in Bacillus megaterium using Escherichia coli K5 glycosyltransferases. International Journal of Biological Macromolecules, 160, 69–76.
Abdulmughni, A., Erichsen, B., Hensel, J., Hannemann, F., & Bernhardt, R. (2020). Improvement of the 25-hydroxyvitamin D3 production in a CYP109A2-expressing Bacillus megaterium system. Journal of Biotechnology, 325, 355–359.
Israni, N., Venkatachalam, P., Gajaraj, B., Varalakshmi, K. N., & Shivakumar, S. (2020). Whey valorization for sustainable polyhydroxyalkanoate production by Bacillus megaterium: Production, characterization and in vitro biocompatibility evaluation. Journal of Environmental Management, 255, 109884.
Kiss, F. M., Lundemo, M. T., Zapp, J., Woodley, J. M., & Bernhardt, R. (2015). Process development for the production of 15 β-hydroxycyproterone acetate using Bacillus megaterium expressing CYP106A2 as whole-cell biocatalyst. Microbial Cell Factories, 14, 1–13.
Ghosh, S., Pawar, H., Pai, O., & Banerjee, U. C. (2014). Microbial transformation of quinic acid to shikimic acid by Bacillus megaterium. Bioresources and Bioprocessing, 1, 1–6.
Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009). Enzymatic assembly of DNA molecules up to several hundred kilobases. Nature Methods, 6, 343–345.
Tadi, S. R. R., Nehru, G., & Sivaprakasam, S. (2021). Combinatorial approach for improved production of whole-cell 3-aminopropionic acid in recombinant Bacillus megaterium: codon optimization, gene duplication and process optimization. 3 Biotech, 11, 1–11.
Lee, H.-N., Shin, W.-S., Seo, S.-Y., Choi, S.-S., Song, J.-S., Kim, J.-Y., Park, J.-H., Lee, D., Kim, S. Y., & Lee, S. J. (2018). Corynebacterium cell factory design and culture process optimization for muconic acid biosynthesis. Scientific Reports, 8, 1–12.
Wang, J.-R., Li, Y.-Y., Liu, D.-N., Liu, J.-S., Li, P., Chen, L.-Z. and Xu, S.-D. (2015) Codon optimization significantly improves the expression level of α-amylase gene from Bacillus licheniformis in Pichia pastoris. BioMed Research International, 2015.
König, L., Hartz, P., Bernhardt, R., & Hannemann, F. (2019). High-yield C11-oxidation of hydrocortisone by establishment of an efficient whole-cell system in Bacillus megaterium. Metabolic Engineering, 55, 59–67.
Elena, C., Ravasi, P., Castelli, M. E., Peirú, S., & Menzella, H. G. (2014). Expression of codon optimized genes in microbial systems: Current industrial applications and perspectives. Frontiers in Microbiology, 5, 21.
Sha, C., Yu, X.-W., Li, F., & Xu, Y. (2013). Impact of gene dosage on the production of lipase from Rhizopus chinensis CCTCC M201021 in Pichia pastoris. Applied Biochemistry and Biotechnology, 169, 1160–1172.
Yang, J., Lu, Z., Chen, J., Chu, P., Cheng, Q., Liu, J., Ming, F., Huang, C., Xiao, A., & Cai, H. (2016). Effect of cooperation of chaperones and gene dosage on the expression of porcine PGLYRP-1 in Pichia pastoris. Applied Microbiology and Biotechnology, 100, 5453–5465.
Liu, Z., Zheng, W., Ye, W., Wang, C., Gao, Y., Cui, W., & Zhou, Z. (2019). Characterization of cysteine sulfinic acid decarboxylase from Tribolium castaneum and its application in the production of β-alanine. Applied Microbiology and Biotechnology, 103, 9443–9453.
Biedendieck, R., Gamer, M., Jaensch, L., Meyer, S., Rohde, M., Deckwer, W.-D., & Jahn, D. (2007). A sucrose-inducible promoter system for the intra-and extracellular protein production in Bacillus megaterium. Journal of Biotechnology, 132, 426–430.
Wang, L., Piao, X., Cui, S., Hu, M., & Tao, Y. (2020). Enhanced production of β-alanine through co-expressing two different subtypes of l-aspartate-α-decarboxylase. Journal of Industrial Microbiology and Biotechnology, 47, 465–474.
Stammen, S., Müller, B. K., Korneli, C., Biedendieck, R., Gamer, M., Franco-Lara, E., & Jahn, D. (2010). High-yield intra-and extracellular protein production using Bacillus megaterium. Applied and Environmental Microbiology, 76, 4037–4046.
Yu, X.-J., Huang, C.-Y., Xu, X.-D., Chen, H., Liang, M.-J., Xu, Z.-X., Xu, H.-X., & Wang, Z. (2020). Protein engineering of a pyridoxal-5′-phosphate-dependent l-aspartate-α-decarboxylase from Tribolium castaneum for β-alanine production. Molecules, 25, 1280.
Phan, A., Ngo, T., & Lenhoff, H. (1982). Spectrophotometric assay for lysine decarbox ylase. Analytical Biochemistry, 120, 193–197.
Lee, S.-G., Hong, S.-P., & Sung, M.-H. (1999). Development of an enzymatic system for the production of dopamine from catechol, pyruvate, and ammonia. Enzyme and Microbial Technology, 25, 298–302.
Ueno, S., Katayama, T., Watanabe, T., Nakajima, K., Hayashi, M., Shigematsu, T., & Fujii, T. (2013). Enzymatic production of γ-aminobutyric acid in soybeans using high hydrostatic pressure and precursor feeding. Bioscience, Biotechnology, and Biochemistry, 77, 706–713.
Xu, J., Zhu, Y., & Zhou, Z. (2021). Systematic engineering of the rate-limiting step of β-alanine biosynthesis in Escherichia coli. Electronic Journal of Biotechnology, 51, 88–94.