Production of 10‐Hydroxy‐2‐decenoic Acid from Decanoic Acid via Whole‐cell Catalysis in Engineered Escherichia coli

ChemSusChem ◽  
2021 ◽  
Author(s):  
Yan Li ◽  
Junqing Wang ◽  
Fen Wang ◽  
Li Wang ◽  
Leilei Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Decanoic Acid ◽  
Decenoic Acid ◽  
Whole Cell ◽  
Whole Cell Catalysis ◽  
Engineered Escherichia Coli

Whole-cell Immobilization of Engineered Escherichia coli JY001 with Barium-alginate for Itaconic Acid Production

2018 ◽  
Vol 23 (4) ◽  
pp. 442-447 ◽  
Author(s):  
Yu-Mi Moon ◽  
Ranjit Gurav ◽  
Junyoung Kim ◽  
Yun-Gi Hong ◽  
Shashi Kant Bhatia ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Itaconic Acid ◽  
Acid Production ◽  
Cell Immobilization ◽  
Whole Cell ◽  
Engineered Escherichia Coli

scholarly journals Generation of two New Macrolactones through Sequential Biotransformation of Dihydroresorcylide

2011 ◽  
Vol 6 (2) ◽  
pp. 1934578X1100600
Author(s):  
Jia Zeng ◽  
Jonathan Valiente ◽  
Jixun Zhan
Keyword(s):  
Escherichia Coli ◽  
Natural Products ◽  
Natural Product ◽  
Beauveria Bassiana ◽  
Natural Product Biosynthesis ◽  
Whole Cell ◽  
E Coli ◽  
Escherichia Coli Bl21 ◽  
Engineered Escherichia Coli

Biotransformation is an effective method to generate new derivatives from natural products. Combination of various enzymes or whole-cell biocatalysts creates new opportunities for natural product biosynthesis. Dihydroresorcylide (1) is a phytotoxic macrolactone from Acremonium aeae. It was first chlorinated at C-11 by an engineered Escherichia coli BL21-CodonPlus (DE3)-RIL/pJZ54 strain that overexpresses a fungal flavin-dependent halogenase, and subsequently glycosylated at 12-OH by Beauveria bassiana ATCC 7159, giving rise to a novel derivative, 11-chloro-4′- O-methyl-12- O-β-D-glucosyl-dihydroresorcylide (3). Although 1 can be converted into a new 4′- O-methyl-glucosylated derivative 4 by B. bassiana, this product cannot be further chlorinated by E. coli BL21-CodonPlus (DE3)-RIL/pJZ54 to afford 3. The sequence of these two biotransformation steps was thus restricted and not interchangeable. This sequential biotransformation approach can be applied to other structurally similar natural products to create novel derivatives.

High-level l-lysine bioconversion into cadaverine with enhanced productivity using engineered Escherichia coli whole-cell biocatalyst

2020 ◽  
Vol 157 ◽  
pp. 107547 ◽  
Author(s):  
Yoong Kit Leong ◽  
Chien-Heng Chen ◽  
Shih-Fang Huang ◽  
Hung-Yi Lin ◽  
Sheng-Feng Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Whole Cell ◽  
Whole Cell Biocatalyst ◽  
Engineered Escherichia Coli ◽  
High Level

Production of p-acetaminophenol by whole-cell catalysis using Escherichia coli overexpressing bacterial aryl acylamidase

2011 ◽  
Vol 34 (4) ◽  
pp. 677-682 ◽  
Author(s):  
Hyeok-Jin Ko ◽  
Won-Gi Bang ◽  
Kyoung Heon Kim ◽  
In-Geol Choi
Keyword(s):  
Escherichia Coli ◽  
Whole Cell ◽  
Aryl Acylamidase ◽  
Whole Cell Catalysis

scholarly journals Biosynthesis of Putrescine from L-arginine Using Engineered Escherichia coli Whole Cells

Catalysts ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 947
Author(s):  
Hongjie Hui ◽  
Yajun Bai ◽  
Tai-Ping Fan ◽  
Xiaohui Zheng ◽  
Yujie Cai
Keyword(s):  
Escherichia Coli ◽  
Biogenic Amine ◽  
Arginine Decarboxylase ◽  
Optimal Concentration ◽  
Optimum Temperature ◽  
Whole Cell ◽  
Whole Cells ◽  
Copy Numbers ◽  
Optimum Ph ◽  
Engineered Escherichia Coli

Putrescine, a biogenic amine, is a highly valued compound in medicine, industry, and agriculture. In this study, we report a whole-cell biocatalytic method in Escherichia coli for the production of putrescine, using L-arginine as the substrate. L-arginine decarboxylase and agmatine ureohydrolase were co-expressed to produce putrescine from L-arginine. Ten plasmids with different copy numbers and ordering of genes were constructed to balance the expression of the two enzymes, and the best strain was pACYCDuet-speB-speA. The optimal concentration of L-arginine was determined to be 20 mM for this strain. The optimum pH of the biotransformation was 9.5, and the optimum temperature was 45 °C; under these conditions, the yield of putrescine was 98%. This whole-cell biocatalytic method appeared to have great potential for the production of putrescine.

scholarly journals Whole-cell catalysis by surface display of fluorinase on Escherichia coli using N-terminal domain of ice nucleation protein

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Xinming Feng ◽  
Miaomiao Jin ◽  
Wei Huang ◽  
Wei Liu ◽  
Mo Xian
Keyword(s):  
Escherichia Coli ◽  
Catalytic Activity ◽  
Industrial Application ◽  
Large Scale ◽  
Surface Display ◽  
Ice Nucleation ◽  
Ice Nucleation Protein ◽  
Whole Cell ◽  
Whole Cell Catalysis

Abstract Background Fluorinases play a unique role in the production of fluorine-containing organic molecules by biological methods. Whole-cell catalysis is a better choice in the large-scale fermentation processes, and over 60% of industrial biocatalysis uses this method. However, the in vivo catalytic efficiency of fluorinases is stuck with the mass transfer of the substrates. Results A gene sequence encoding a protein with fluorinase function was fused to the N-terminal of ice nucleation protein, and the fused fluorinase was expressed in Escherichia coli BL21(DE3) cells. SDS-PAGE and immunofluorescence microscopy were used to demonstrate the surface localization of the fusion protein. The fluorinase displayed on the surface showed good stability while retaining the catalytic activity. The engineered E.coli with surface-displayed fluorinase could be cultured to obtain a larger cell density, which was beneficial for industrial application. And 55% yield of 5′-fluorodeoxyadenosine (5′-FDA) from S-adenosyl-L-methionine (SAM) was achieved by using the whole-cell catalyst. Conclusions Here, we created the fluorinase-containing surface display system on E.coli cells for the first time. The fluorinase was successfully displayed on the surface of E.coli and maintained its catalytic activity. The surface display provides a new solution for the industrial application of biological fluorination. Graphical Abstract

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