scholarly journals The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

Catalysts ◽  
2017 ◽  
Vol 7 (9) ◽  
pp. 251 ◽  
Author(s):  
Hyunwoo Jeon ◽  
Sanghan Yoon ◽  
Md Ahsan ◽  
Sihyong Sung ◽  
Geon-Hee Kim ◽  
...  
Keyword(s):  
Kinetic Resolution ◽  
Nadh Oxidase ◽  
Whole Cell ◽  
Whole Cell Biocatalyst ◽  
Amine Dehydrogenase ◽  
Racemic Amines

scholarly journals Efficient 2,3-Butanediol/Acetoin Production Using Whole-Cell Biocatalyst with a New Nadh/Nad(+) Regeneration System

Catalysts ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1422
Author(s):  
Yaping Wang ◽  
Yanhong Peng ◽  
Xiaoyan Liu ◽  
Ronghua Zhou ◽  
Xianqing Liao ◽  
...  
Keyword(s):  
Formate Dehydrogenase ◽  
Target Genes ◽  
Nadh Oxidase ◽  
Expression System ◽  
Regeneration System ◽  
Nadh Regeneration ◽  
Whole Cell ◽  
Whole Cell Biocatalyst ◽  
Acetoin Production ◽  
Butanediol Dehydrogenase

An auto-inducing expression system was developed that could express target genes in S. marcescens MG1. Using this system, MG1 was constructed as a whole-cell biocatalyst to produce 2,3-butanediol/acetoin. Formate dehydrogenase (FDH) and 2,3-butanediol dehydrogenase were expressed together to build an NADH regeneration system to transform diacetyl to 2,3-butanediol. After fermentation, the extract of recombinant S. marcescens MG1ABC (pETDuet-bdhA-fdh) showed 2,3-BDH activity of 57.8 U/mg and FDH activity of 0.5 U/mg. And 27.95 g/L of 2,3-BD was achieved with a productivity of 4.66 g/Lh using engineered S. marcescens MG1(Pswnb+pETDuet-bdhA-fdh) after 6 h incubation. Next, to produce 2,3-butanediol from acetoin, NADH oxidase and 2,3-butanediol dehydrogenase from Bacillus subtilis were co-expressed to obtain a NAD+ regeneration system. After fermentation, the recombinant strain S. marcescens MG1ABC (pSWNB+pETDuet-bdhA-yodC) showed AR activity of 212.4 U/mg and NOX activity of 150.1 U/mg. We obtained 44.9 g/L of acetoin with a productivity of 3.74 g/Lh using S. marcescens MG1ABC (pSWNB+pETDuet-bdhA-yodC). This work confirmed that S. marcescens could be designed as a whole-cell biocatalyst for 2,3-butanediol and acetoin production.

scholarly journals Industrial kinetic resolution of d,l-pantolactone by an immobilized whole-cell biocatalyst

RSC Advances ◽  
2021 ◽  
Vol 11 (48) ◽  
pp. 30373-30376
Author(s):  
Qiu-Hua Zhang ◽  
Liu Yang ◽  
Yi-Bin Tang ◽  
Liu-Nv Huang ◽  
Wen-Fang Luo
Keyword(s):  
Pichia Pastoris ◽  
Calcium Alginate ◽  
Kinetic Resolution ◽  
Whole Cell ◽  
Whole Cells ◽  
Whole Cell Biocatalyst ◽  
Alginate Gels ◽  
Calcium Alginate Gels ◽  
Immobilized Whole Cells

Immobilized whole-cells of Pichia pastoris harboring recombinant d-lactonase were entrapped in calcium alginate gels and used as an efficient biocatalyst for catalytic kinetic resolution of d,l-pantolactone.

scholarly journals Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

Catalysts ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 600 ◽  
Author(s):  
Mahesh D. Patil ◽  
Sanghan Yoon ◽  
Hyunwoo Jeon ◽  
Taresh P. Khobragade ◽  
Sharad Sarak ◽  
...  
Keyword(s):  
Kinetic Resolution ◽  
Product Inhibition ◽  
Oxidative Deamination ◽  
Whole Cells ◽  
Alanine Dehydrogenase ◽  
Enzyme Cascade ◽  
Wide Range ◽  
Enzymatic Systems ◽  
Amine Dehydrogenase ◽  
Racemic Amines

Amine dehydrogenases (AmDHs) efficiently catalyze the NAD(P)H-dependent asymmetric reductive amination of prochiral carbonyl substrates with high enantioselectivity. AmDH-catalyzed oxidative deamination can also be used for the kinetic resolution of racemic amines to obtain enantiopure amines. In the present study, kinetic resolution was carried out using a coupled-enzyme cascade consisting of AmDH and alanine dehydrogenase (AlaDH). AlaDH efficiently catalyzed the conversion of pyruvate to alanine, thus recycling the nicotinamide cofactors and driving the reaction forward. The ee values obtained for the kinetic resolution of 25 and 50 mM rac-α-methylbenzylamine using the purified enzymatic systems were only 54 and 43%, respectively. The use of whole-cells apparently reduced the substrate/product inhibition, and the use of only 30 and 40 mgDCW/mL of whole-cells co-expressing AmDH and AlaDH efficiently resolved 100 mM of rac-2-aminoheptane and rac-α-methylbenzylamine into the corresponding enantiopure (S)-amines. Furthermore, the applicability of the reaction protocol demonstrated herein was also successfully tested for the efficient kinetic resolution of wide range of racemic amines.

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.

Antityrosinase Mechanism and Antimelanogenic Effect of Arbutin Esters Synthesis Catalyzed by Whole-Cell Biocatalyst

2021 ◽  
Vol 69 (14) ◽  
pp. 4243-4252
Author(s):  
Haixia Xu ◽  
Xiaofeng Li ◽  
Xuan Xin ◽  
Lan Mo ◽  
Yucong Zou ◽  
...  
Keyword(s):  
Whole Cell ◽  
Whole Cell Biocatalyst
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