Enhanced conversion of L-lysine to L-pipecolic acid using a recombinant Escherichia coli containing lysine cyclodeaminase as whole-cell biocatalyst

2015 ◽  
Vol 117 ◽  
pp. 75-80 ◽  
Author(s):  
Hanxiao Ying ◽  
Jing Wang ◽  
Zhen Wang ◽  
Jiao Feng ◽  
Kequan Chen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Escherichia Coli ◽  
Pipecolic Acid ◽  
Whole Cell ◽  
Whole Cell Biocatalyst

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.

Characterization of a recombinant Escherichia coli TOP10 [pQR239] whole-cell biocatalyst for stereoselective Baeyer–Villiger oxidations

2003 ◽  
Vol 32 (3-4) ◽  
pp. 347-355 ◽  
Author(s):  
Steven D Doig ◽  
Helen Simpson ◽  
Veronique Alphand ◽  
Roland Furstoss ◽  
John M Woodley
Keyword(s):  
Escherichia Coli ◽  
Recombinant Escherichia Coli ◽  
Whole Cell ◽  
Whole Cell Biocatalyst

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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