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Open AccessArticle

High-Level Conversion of l-lysine into Cadaverine by Escherichia coli Whole Cell Biocatalyst Expressing Hafnia alvei l-lysine Decarboxylase

1
Bio-Based Chemistry Research Center, Advanced Convergent Chemistry Division, Korea Research Institute of Chemical Technology, P.O. Box 107, 141 Gajeong-ro, Yuseong-gu, Daejeon 34114, Korea
2
Division of Chemical Engineering and Materials Science, Ewha Womans University, 52 Ewhayeodae-gil, Seodaemun-gu, Seoul 03760, Korea
3
Department of Biological and Chemical Engineering, Hongik University, 2639 Sejong-ro, Sinan-ri, Jochiwon-eup, Sejong-si 30016, Korea
4
Bioprocess R&D Center, DAESANG Corp., Icheon-si, Gyeonggi-do 17384, Korea
5
Lotte Chemical, 115 Gajeongbuk-ro, Yuseong-gu, Daejeon 34110, Korea
6
Department of Chemistry, KAIST, 291, Daehak-ro, Yuseong-gu, Daejeon 34141, Korea
*
Authors to whom correspondence should be addressed.
Hee Taek Kim and Kei-Anne Baritugo contributed equally to this work.
Polymers 2019, 11(7), 1184; https://doi.org/10.3390/polym11071184
Received: 16 June 2019 / Revised: 3 July 2019 / Accepted: 5 July 2019 / Published: 14 July 2019
(This article belongs to the Special Issue Microbial Production and Application of Biopolymers)
Cadaverine is a C5 diamine monomer used for the production of bio-based polyamide 510. Cadaverine is produced by the decarboxylation of l-lysine using a lysine decarboxylase (LDC). In this study, we developed recombinant Escherichia coli strains for the expression of LDC from Hafnia alvei. The resulting recombinant XBHaLDC strain was used as a whole cell biocatalyst for the high-level bioconversion of l-lysine into cadaverine without the supplementation of isopropyl β-d-1-thiogalactopyranoside (IPTG) for the induction of protein expression and pyridoxal phosphate (PLP), a key cofactor for an LDC reaction. The comparison of results from enzyme characterization of E. coli and H. alvei LDC revealed that H. alvei LDC exhibited greater bioconversion ability than E. coli LDC due to higher levels of protein expression in all cellular fractions and a higher specific activity at 37 °C (1825 U/mg protein > 1003 U/mg protein). The recombinant XBHaLDC and XBEcLDC strains were constructed for the high-level production of cadaverine. Recombinant XBHaLDC produced a 1.3-fold higher titer of cadaverine (6.1 g/L) than the XBEcLDC strain (4.8 g/L) from 10 g/L of l-lysine. Furthermore, XBHaLDC, concentrated to an optical density (OD600) of 50, efficiently produced 136 g/L of cadaverine from 200 g/L of l-lysine (97% molar yield) via an IPTG- and PLP-free whole cell bioconversion reaction. Cadaverine synthesized via a whole cell biocatalyst reaction using XBHaLDC was purified to polymer grade, and purified cadaverine was successfully used for the synthesis of polyamide 510. In conclusion, an IPTG- and PLP-free whole cell bioconversion process of l-lysine into cadaverine, using recombinant XBHaLDC, was successfully utilized for the production of bio-based polyamide 510, which has physical and thermal properties similar to polyamide 510 synthesized from chemical-grade cadaverine. View Full-Text
Keywords: cadaverine; IPTG- and PLP-free whole cell biocatalyst reaction; lysine decarboxylase; Hafnia alvei; polyamide 510 cadaverine; IPTG- and PLP-free whole cell biocatalyst reaction; lysine decarboxylase; Hafnia alvei; polyamide 510
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Kim, H.T.; Baritugo, K.-A.; Oh, Y.H.; Kang, K.-H.; Jung, Y.J.; Jang, S.; Song, B.K.; Kim, I.-K.; Lee, M.O.; Hwang, Y.T.; Park, K.; Park, S.J.; Joo, J.C. High-Level Conversion of l-lysine into Cadaverine by Escherichia coli Whole Cell Biocatalyst Expressing Hafnia alvei l-lysine Decarboxylase. Polymers 2019, 11, 1184.

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