The production of enantiopure D-lysine from L-lysine by a two-strain coupled system

doi:10.1016/j.cjche.2020.06.020

Chinese Journal of Chemical Engineering ›› 2020, Vol. 28 ›› Issue (11): 2832-2836.DOI: 10.1016/j.cjche.2020.06.020

Previous Articles Next Articles

The production of enantiopure D-lysine from L-lysine by a two-strain coupled system

Sheng Xu, Xiaolu Lu, Xin Wang, Zhen Gao, Kequan Chen, Pingkai Ouyang

State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, China

Received:2020-01-09 Revised:2020-05-09 Online:2020-12-31 Published:2020-11-28
Contact: Zhen Gao
Supported by:
The financial supports from the National Natural Science Foundation of China (Grant No. 21908099), the National Key Research and Development Program of China (Grant No. 2016YFA0204300), Key Research and Development Program (Social Development) Project Jiangsu Province (Grant No. BE2018730), the Natural Science Research Projects of Colleges and Universities in Jiangsu Province (Grant No. 18KJB530009), and the Jiangsu Synergetic Innovation Center for Advanced Bio-Manufacture (Grant No. XTB1802, Grant No. XTE1846) are gratefully acknowledged.

The production of enantiopure D-lysine from L-lysine by a two-strain coupled system

Sheng Xu, Xiaolu Lu, Xin Wang, Zhen Gao, Kequan Chen, Pingkai Ouyang

State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, China

通讯作者: Zhen Gao
基金资助:
The financial supports from the National Natural Science Foundation of China (Grant No. 21908099), the National Key Research and Development Program of China (Grant No. 2016YFA0204300), Key Research and Development Program (Social Development) Project Jiangsu Province (Grant No. BE2018730), the Natural Science Research Projects of Colleges and Universities in Jiangsu Province (Grant No. 18KJB530009), and the Jiangsu Synergetic Innovation Center for Advanced Bio-Manufacture (Grant No. XTB1802, Grant No. XTE1846) are gratefully acknowledged.

Abstract

Abstract: The microbial production of D-lysine to replace chemical approach has gained great interest with the rising concerns over the environment. Here, we employed recombinant E. coli strain BL21-LYR with lysine racemase and strain BL-22A-RB-YB with L-lysine monooxygenase and 5-aminovaleramide amidohydrolase to establish a two-strain coupling whole-cell bioconversion system for D-lysine production from L-lysine. To improve the optical purity of D-lysine, the optimal reaction condition for resolution of DL-lysine after the racemization was investigated. The specificity of BL-22A-RB-YB for L-lysine and the effects of reaction condition on bioconversion efficiency of whole-cell were accordingly determined. Under the optimal condition, a maximum 53.5 g·L^-1 Dlysine and 48.2 g·L^-1 5-AVA were obtained with yield of 47.4% and 42.3%, respectively, by the microbial racemization and asymmetric degradation process. The final D-lysine enantiomeric excess was over 99%. Meanwhile, a valuable compound 5-aminovaleric acid was synthesized with the production of D-lysine, indicating the economic feasibility of the two-strain coupling system.

Key words: D-Lysine, Microbial resolution, Two-strain coupling system

摘要： The microbial production of D-lysine to replace chemical approach has gained great interest with the rising concerns over the environment. Here, we employed recombinant E. coli strain BL21-LYR with lysine racemase and strain BL-22A-RB-YB with L-lysine monooxygenase and 5-aminovaleramide amidohydrolase to establish a two-strain coupling whole-cell bioconversion system for D-lysine production from L-lysine. To improve the optical purity of D-lysine, the optimal reaction condition for resolution of DL-lysine after the racemization was investigated. The specificity of BL-22A-RB-YB for L-lysine and the effects of reaction condition on bioconversion efficiency of whole-cell were accordingly determined. Under the optimal condition, a maximum 53.5 g·L^-1 Dlysine and 48.2 g·L^-1 5-AVA were obtained with yield of 47.4% and 42.3%, respectively, by the microbial racemization and asymmetric degradation process. The final D-lysine enantiomeric excess was over 99%. Meanwhile, a valuable compound 5-aminovaleric acid was synthesized with the production of D-lysine, indicating the economic feasibility of the two-strain coupling system.

关键词: D-Lysine, Microbial resolution, Two-strain coupling system

Sheng Xu, Xiaolu Lu, Xin Wang, Zhen Gao, Kequan Chen, Pingkai Ouyang. The production of enantiopure D-lysine from L-lysine by a two-strain coupled system[J]. Chinese Journal of Chemical Engineering, 2020, 28(11): 2832-2836.

Sheng Xu, Xiaolu Lu, Xin Wang, Zhen Gao, Kequan Chen, Pingkai Ouyang. The production of enantiopure D-lysine from L-lysine by a two-strain coupled system[J]. 中国化学工程学报, 2020, 28(11): 2832-2836.

References

[1] W.C. Shen, X.T. Du, E.P. Feener, H.J.P. Ryser, The intracellular release of methotrexate from a synthetic drug carrier system targeted to fc receptor-bearing cells, J. Control. Release 10(1989) 89-96.
[2] E. Takahashi, M. Furui, H. Seko, T. Shibatani, D-Lysine production from L-lysine by successive chemical racemization and microbial asymmetric degradation, Appl. Microbiol. Biotechnol. 47(1997) 347-351.
[3] H.M. Kaminski, J.B. Feix, Effects of D-lysine substitutions on the activity and selectivity of antimicrobial peptide CM15, Polymers (Basel) 3(2011) 2088-2106.
[4] Y. Liu, Q. Jiao, X. Yin, Preparation of D-lysine by chemical reaction and microbial asymmetric transformation, Front. Chem. Eng. China 2(2008) 40-43.
[5] Y. Lu, S. Wu, H. Zhang, Q. Liu, Q. Jiao, J. Liu, Production of D-lysine catalyzed by a two-step biocatalytic cascade of amino acid racemase and lysine decarboxylase, Fine Chem. 32(2015) 873-877.
[6] X. Wang, L. Yang, W. Cao, H. Ying, K. Chen, P. Ouyang, Efficient production of enantiopure D-lysine from L-lysine by a two-enzyme cascade system, Catal 6(2016) 168-179.
[7] S. Singh, B.K. Gogoi, R.L. Bezbaruah, Racemic resolution of some DL-amino acids using Aspergillus fumigatus L-amino acid oxidase, Curr. Microbiol. 63(2011) 94-99.
[8] A.V. Pukin, C.G. Boeriu, E.L. Scott, J.P.M. Sanders, M.C.R. Franssen, An efficient enzymatic synthesis of 5-aminovaleric acid, J. Mol. Catal. B Enzym. 65(2010) 58-62.
[9] J.B. Williams, T.M. Chapman, D.M. Hercules, Synthesis of discrete mass poly(butylene glutarate) oligomers, Macromolecules 36(11) (2003) 3898-3908.
[10] J. Adkins, J. Jordan, D.R. Nielsen, Engineering Escherichia coli for renewable production of the 5-carbon polyamide building-blocks 5-aminovalerate and glutarate, Biotechnol. Bioeng. 110(2013) 1726-1734.
[11] A.F. Baldwin, R. Ma, A. Mannodi-Kanakkithodi, T.D. Huan, C. Wang, M. Tefferi, J.E. Marszalek, M. Cakmak, Y. Cao, R. Ramprasad, G.A. Sotzing, Poly(dimethyltin glutarate) as a prospective material for high dielectric applications, Adv. Mater. 27(2) (2015) 346-351.
[12] X. Wang, P. Cai, K. Chen, P. Ouyang, Efficient production of 5-aminovalerate from Llysine by engineered Escherichia coli whole-cell biocatalysts, J. Mol. Catal. B Enzym. 134(2016) 115-121.
[13] X. Zhang, Y. Ma, Y.H. Liu, Z.G. Cui, F. Wang, Synthesis of octyl glucoside from glucose catalyzed by attapulgite immobilized β-glucosidase, Mod. Chem. Ind. 36(2016) 132-135137.
[14] W. Ma, W. Cao, H. Zhang, K. Chen, Y. Li, P. Ouyang, Enhanced cadaverine production from l-lysine using recombinant Escherichia coli co-overexpressing CadA and CadB, Biotechnol. Lett. 37(2015) 799-806.
[15] C. Andreini, I. Bertini, G. Cavallaro, G.L. Holliday, J.M. Thornton, Metal ions in biological catalysis:From enzyme databases to general principles, J. Biol. Inorg. Chem. 13(2008) 1205-1218.
[16] J.W. Szostak, D.P. Bartel, P.L. Luisi, Synthesizing life, Nature. (2001) 387-390.
[17] H. Chung, J.E. Yang, J.Y. Ha, T.U. Chae, J.H. Shin, M. Gustavsson, S.Y. Lee, Bio-based production of monomers and polymers by metabolically engineered microorganisms, Curr. Opin. Biotechnol. 36(2015) 73-84.
[18] M. Friedman, C.E. Levin, Nutritional and medicinal aspects of D-amino acids, Amino Acids (2012) 1553-1582.
[19] O. Revelles, M. Espinosa-Urgel, T. Fuhrer, U. Sauer, J.L. Ramos, Multiple and interconnected pathways for l-lysine catabolism in Pseudomonas putida KT2440, J. Bacteriol. 187(2005) 7500-7510.
[20] P. Liu, H. Zhang, M. Lv, M. Hu, Z. Li, C. Gao, P. Xu, C. Ma, Enzymatic production of 5-aminovalerate from l-lysine using l-lysine monooxygenase and 5-aminovaleramide amidohydrolase, Sci. Rep. 4(2015) 5657.
[21] M. Cánovas, T. Torroglosa, J.L. Iborra, Permeabilization of Escherichia coli cells in the biotransformation of trimethylammonium compounds into L-carnitine, Enzym. Microb. Technol. 37(3) (2005) 300-308.
[22] H. Li, S. Yin, X. Zhang, X. Zhang, H. Li, J. Shi, Z. Xu, Enhanced 3β,7α,15α-Trihydroxy-5-Androsten-17-one production from Dehydroepiandrosterone by Colletotrichum lini ST-1 resting cells with Tween-80, Appl. Biochem. Biotechnol. 178(2016) 91-100.

The production of enantiopure D-lysine from L-lysine by a two-strain coupled system

The production of enantiopure D-lysine from L-lysine by a two-strain coupled system

PDF (PC)

Knowledge

Abstract

Cite this article

share this article

References

Related Articles 0

Recommended Articles

Metrics

Comments