scholarly journals Ultrasound-assisted l-cysteine whole-cell bioconversion by recombinant Escherichia coli with tryptophan synthase

2021 ◽  
Vol 10 (1) ◽  
pp. 842-850
Author(s):  
Lisheng Xu ◽  
Furu Wu ◽  
Tingting Li ◽  
Xingtao Zhang ◽  
Qiong Chen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell System ◽  
Tryptophan Synthase ◽  
Cysteine Biosynthesis ◽  
Optimal Conditions ◽  
Whole Cell ◽  
G Cells ◽  
Biological Transformation ◽  
Ultrasound Assisted ◽  
Whole Cell Bioconversion

Abstract l-Cysteine is widely used in food, medicine, and cosmetics. In this study, a recombinant Escherichia coli whole-cell system with tryptophan synthase was used to complete the biological transformation of l-serine to l-cysteine, and bioconversion of l-cysteine was investigated by tryptophan synthase. The biotransformation of l-cysteine was optimized by response surface methodology. The optimal conditions obtained are 0.13 mol·L−1 l-serine, 75 min, 130 W ultrasound operation, where the V max of tryptophan synthase is 25.27 ± 0.16 (mmol·h−1·(g-cells)−1). The V max of tryptophan synthase for the biosynthesis without ultrasound is 12.91 ± 0.34 (mmol·h−1·(g-cells)−1). Kinetic analysis of the recombinant Escherichia coli whole-cell system with tryptophan synthase also showed that under the ultrasound treatment, the K m values of l-cysteine biosynthesis increase from 1.342 ± 0.11 mM for the shaking biotransformation to 2.555 ± 0.13 mM for ultrasound operation. The yield of l-cysteine reached 91% after 75 min of treatment after 130 W ultrasound, which is 1.9-fold higher than no ultrasound.

scholarly journals Ultrasound-assisted d-tartaric acid whole-cell bioconversion by recombinant Escherichia coli

2018 ◽  
Vol 42 ◽  
pp. 11-17 ◽  
Author(s):  
Weiliang Dong ◽  
Fenglian Zhao ◽  
Fengxue Xin ◽  
Aiyong He ◽  
Yue Zhang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Tartaric Acid ◽  
Recombinant Escherichia Coli ◽  
Whole Cell ◽  
Ultrasound Assisted ◽  
Whole Cell Bioconversion

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 Production of itaconate by whole-cell bioconversion of citrate mediated by expression of multiple cis-aconitate decarboxylase (cadA) genes in Escherichia coli

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Junyoung Kim ◽  
Hyung-Min Seo ◽  
Shashi Kant Bhatia ◽  
Hun-Seok Song ◽  
Jung-Ho Kim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Whole Cell ◽  
Whole Cell Bioconversion

scholarly journals Enhancement of pipecolic acid production by the expression of multiple lysine cyclodeaminase in the Escherichia coli whole-cell system

Authorea ◽  
2020 ◽  
Author(s):  
Yeong Hoon Han ◽  
Tae Rim Choi ◽  
Ye Lim Park ◽  
Jun Young Park ◽  
Hun suk Song ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acid Production ◽  
Cell System ◽  
Pipecolic Acid ◽  
Whole Cell

scholarly journals Ultrasound-assisted (R)-phenylephrine whole-cell bioconversion by S. marcescens N10612

2015 ◽  
Vol 26 ◽  
pp. 415-421 ◽  
Author(s):  
Chi-Zong Zang ◽  
Shu-Chen Kan ◽  
Chiung-Wen Yeh ◽  
Chia-Chi Lin ◽  
Chwen-Jen Shieh ◽  
...  
Keyword(s):  
Whole Cell ◽  
Ultrasound Assisted ◽  
Whole Cell Bioconversion

scholarly journals A CYP21A2 based whole-cell system in Escherichia coli for the biotechnological production of premedrol

2015 ◽  
Vol 14 (1) ◽  
Author(s):  
Simone Brixius-Anderko ◽  
Lina Schiffer ◽  
Frank Hannemann ◽  
Bernd Janocha ◽  
Rita Bernhardt
Keyword(s):  
Escherichia Coli ◽  
Cell System ◽  
Biotechnological Production ◽  
Whole Cell

Enhancement of pipecolic acid production by the expression of multiple lysine cyclodeaminase in the Escherichia coli whole-cell system

2020 ◽  
Vol 140 ◽  
pp. 109643
Author(s):  
Yeong-Hoon Han ◽  
Tae-Rim Choi ◽  
Ye-Lim Park ◽  
Jun Young Park ◽  
Hun-Suk Song ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acid Production ◽  
Cell System ◽  
Pipecolic Acid ◽  
Whole Cell

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.

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