Development of a Whole-Cell Biocatalyst/Biosensor by Display of Multiple Heterologous Proteins on the Escherichia coli Cell Surface for the Detoxification and Detection of Organophosphates

2013 ◽  
Vol 61 (32) ◽  
pp. 7810-7816 ◽  
Author(s):  
Ruihua Liu ◽  
Chao Yang ◽  
Yingming Xu ◽  
Ping Xu ◽  
Hong Jiang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Coli Cell ◽  
Heterologous Proteins ◽  
Whole Cell ◽  
Whole Cell Biocatalyst

scholarly journals Display of Multimeric Antimicrobial Peptides on the Escherichia coli Cell Surface and Its Application as Whole-Cell Antibiotics

PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e58997 ◽  
Author(s):  
Ju Ri Shin ◽  
Ki Jung Lim ◽  
Da Jung Kim ◽  
Ju Hyun Cho ◽  
Sun Chang Kim
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Antimicrobial Peptides ◽  
Coli Cell ◽  
Whole Cell

Expressing Xylanases in Escherichia Coli by Cell Surface Display

2013 ◽  
Vol 634-638 ◽  
pp. 965-969
Author(s):  
Mei Na Zhao ◽  
Zongbao Zheng ◽  
Tao Chen
Keyword(s):  
Escherichia Coli ◽  
Cell Surface ◽  
Consolidated Bioprocessing ◽  
Surface Display ◽  
Cell Surface Display ◽  
Whole Cell ◽  
E Coli ◽  
Metabolic Burden ◽  
Whole Cell Biocatalyst ◽  
Anchor Proteins

In this research, xylan was utilized by a recombinant whole cell biocatalyst, which was developed by expressing three xylanases — β-xylosidase, endoxylanase, and α-arabinofuranosidase — on the surface of the E. coli BL21 (DE3). The xylanases were displayed on the surface of the cells by fusing with anchor proteins, Blc. The assimilation of xylan by cell surface display was the first step in the consolidated bioprocessing (CBP). This result shows that the engineering strains could be endowed with the ability to assimilate xylan. The co-display engineering strains utilized xylan and expressed less metabolic burden than the engineering strains secreting extracellular xylanases.

scholarly journals Tuning a bi-enzymatic cascade reaction in Escherichia coli to facilitate NADPH regeneration for ε-caprolactone production

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Jinghui Xiong ◽  
Hefeng Chen ◽  
Ran Liu ◽  
Hao Yu ◽  
Min Zhuo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Regeneration System ◽  
Nadph Regeneration ◽  
Whole Cell ◽  
Cyclohexanone Monooxygenase ◽  
Ribosome Binding ◽  
Ribosome Binding Sites ◽  
Whole Cell Biocatalyst ◽  
Substrate Tolerance

Abstractε-Caprolactone is a monomer of poly(ε-caprolactone) which has been widely used in tissue engineering due to its biodegradability and biocompatibility. To meet the massive demand for this monomer, an efficient whole-cell biocatalytic approach was constructed to boost the ε-caprolactone production using cyclohexanol as substrate. Combining an alcohol dehydrogenase (ADH) with a cyclohexanone monooxygenase (CHMO) in Escherichia coli, a self-sufficient NADPH-cofactor regeneration system was obtained. Furthermore, some improved variants with the better substrate tolerance and higher catalytic ability to ε-caprolactone production were designed by regulating the ribosome binding sites. The best mutant strain exhibited an ε-caprolactone yield of 0.80 mol/mol using 60 mM cyclohexanol as substrate, while the starting strain only got a conversion of 0.38 mol/mol when 20 mM cyclohexanol was supplemented. The engineered whole-cell biocatalyst was used in four sequential batches to achieve a production of 126 mM ε-caprolactone with a high molar yield of 0.78 mol/mol.

Permeabilizing Escherichia coli for whole cell biocatalyst with enhanced biotransformation ability from l-glutamate to GABA

2014 ◽  
Vol 107 ◽  
pp. 39-46 ◽  
Author(s):  
Wei-rui Zhao ◽  
Jun Huang ◽  
Chun-long Peng ◽  
Sheng Hu ◽  
Pi-yu Ke ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Whole Cell ◽  
Whole Cell Biocatalyst

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.

scholarly journals Enhanced production of optical (S)-acetoin by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration

RSC Advances ◽  
2018 ◽  
Vol 8 (53) ◽  
pp. 30512-30519 ◽  
Author(s):  
Jian-Xiu Li ◽  
Yan-Yan Huang ◽  
Xian-Rui Chen ◽  
Qi-Shi Du ◽  
Jian-Zong Meng ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Escherichia Coli ◽  
Nadh Regeneration ◽  
Whole Cell ◽  
Enhanced Production ◽  
Whole Cell Biocatalyst ◽  
Regeneration Systems

Enhanced production of optical (S)-acetoin by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration systems.

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