Preparation of 11-hexyloxy-9-undecenoic acid from crude castor oil hydrolysates by recombinant Escherichia coli expressing alcohol dehydrogenase and Baeyer–Villiger monooxygenase

2016 ◽  
Vol 51 (3) ◽  
pp. 362-368 ◽  
Author(s):  
Jae Hoon Lee ◽  
Sung Hee Choi ◽  
In Yeub Hwang ◽  
Jin Byung Park ◽  
Ssangsoo Han ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Castor Oil ◽  
Recombinant Escherichia Coli ◽  
Undecenoic Acid

scholarly journals Suitability of Recombinant Escherichia coli and Pseudomonas putida Strains for Selective Biotransformation of m-Nitrotoluene by Xylene Monooxygenase

2005 ◽  
Vol 71 (11) ◽  
pp. 6624-6632 ◽  
Author(s):  
Daniel Meyer ◽  
Bernard Witholt ◽  
Andreas Schmid
Keyword(s):  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Pseudomonas Putida ◽  
Aromatic Amines ◽  
Major Effect ◽  
Recombinant Escherichia Coli ◽  
Reaction Products ◽  
E Coli ◽  
Nitrobenzoic Acid ◽  
Nitrobenzyl Alcohol

ABSTRACT Escherichia coli JM101(pSPZ3), containing xylene monooxygenase (XMO) from Pseudomonas putida mt-2, catalyzes specific oxidations and reductions of m-nitrotoluene and derivatives thereof. In addition to reactions catalyzed by XMO, we focused on biotransformations by native enzymes of the E. coli host and their effect on overall biocatalyst performance. While m-nitrotoluene was consecutively oxygenated to m-nitrobenzyl alcohol, m-nitrobenzaldehyde, and m-nitrobenzoic acid by XMO, the oxidation was counteracted by an alcohol dehydrogenase(s) from the E. coli host, which reduced m-nitrobenzaldehyde to m-nitrobenzyl alcohol. Furthermore, the enzymatic background of the host reduced the nitro groups of the reactants resulting in the formation of aromatic amines, which were shown to effectively inhibit XMO in a reversible fashion. Host-intrinsic oxidoreductases and their reaction products had a major effect on the activity of XMO during biocatalysis of m-nitrotoluene. P. putida DOT-T1E and P. putida PpS81 were compared to E. coli JM101 as alternative hosts for XMO. These promising strains contained an additional dehydrogenase that oxidized m-nitrobenzaldehyde to the corresponding acid but catalyzed the formation of XMO-inhibiting aromatic amines at a significantly lower level than E. coli JM101.

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