Characterization of a Whole-Cell Biotransformation Using a Constitutive Lysine Decarboxylase from Escherichia coli for the High-Level Production of Cadaverine from Industrial Grade l-Lysine

2018 ◽  
Vol 185 (4) ◽  
pp. 909-924 ◽  
Author(s):  
Jihyun Shin ◽  
Jeong Chan Joo ◽  
Eunji Lee ◽  
Sung Min Hyun ◽  
Hyun Joong Kim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lysine Decarboxylase ◽  
Whole Cell ◽  
Industrial Grade ◽  
Whole Cell Biotransformation ◽  
High Level ◽  
Level Production

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

Polymers ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 1184 ◽  
Author(s):  
Kim ◽  
Baritugo ◽  
Oh ◽  
Kang ◽  
Jung ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Expression ◽  
Pyridoxal Phosphate ◽  
Lysine Decarboxylase ◽  
Hafnia Alvei ◽  
Whole Cell ◽  
E Coli ◽  
Whole Cell Biocatalyst ◽  
High Level ◽  
Whole Cell Bioconversion

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.

Efficient process development for high‐level production, purification, formulation, and characterization of recombinant mecasermin in Escherichia coli

2020 ◽  
Author(s):  
Mohammad Reza Mofid ◽  
Valiollah Babaeipour ◽  
Sevda Jafari ◽  
Leila Haddad ◽  
Sharareh Moghim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Process Development ◽  
Efficient Process ◽  
High Level ◽  
Level Production

High-level production and one-step purification of biologically active human growth hormone in Escherichia coli

Gene ◽  
1995 ◽  
Vol 165 (2) ◽  
pp. 303-306 ◽  
Author(s):  
Reema Mukhija ◽  
Prithy Rupa ◽  
Devika Pillai ◽  
Lalit C. Garg
Keyword(s):  
Escherichia Coli ◽  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Biologically Active ◽  
One Step ◽  
High Level ◽  
Level Production

scholarly journals Characterization of P450 FcpC, the Enzyme Responsible for Bioconversion of Diosgenone to Isonuatigenone in Streptomyces virginiae IBL-14

2009 ◽  
Vol 75 (12) ◽  
pp. 4202-4205 ◽  
Author(s):  
Wei Wang ◽  
Feng-Qing Wang ◽  
Dong-Zhi Wei
Keyword(s):  
Escherichia Coli ◽  
Electron Transfer ◽  
Cytochrome P450 ◽  
Cytochrome P450 Monooxygenase ◽  
P450 Monooxygenase ◽  
Whole Cell ◽  
Electron Transfer Chain ◽  
Streptomyces Virginiae ◽  
Transfer Chain

ABSTRACT A new cytochrome P450 monooxygenase, FcpC, from Streptomyces virginiae IBL-14 has been identified. This enzyme is found to be responsible for the bioconversion of a pyrano-spiro steroid (diosgenone) to a rare nuatigenin-type spiro steroid (isonuatigenone), which is a novel C-25-hydroxylated diosgenone derivative. A whole-cell P450 system was developed for the production of isonuatigenone via the expression of the complete three-component electron transfer chain in an Escherichia coli strain.

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