2015
DOI: 10.1007/s11746-015-2694-4
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13‐Hydroxy‐9Z,11E‐Octadecadienoic Acid Production by Recombinant Cells Expressing Burkholderia thailandensis 13‐Lipoxygenase

Abstract: Linoleate 13-lipoxygenase from Burkholderia thailandensis was expressed in Escherichia coli for the production of 13-hydroxyoctadecadienoic acid (13-HODE), an antiseptic emulsifier. Linoleate 13-lipoxygenase in cells had higher thermal stability than the purified enzyme. To increase 13-HODE production, recombinant cells were permeabilized by solvents, detergents, salts, and other chemicals. The enzymatic activity in cells was the highest for permeabilized cells treated with 0.5 M NaCl among the permeabilizers … Show more

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Cited by 17 publications
(12 citation statements)
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“…Oxygenases such as A. nidulans 5,8-LDS 10 and Burkholderia thailandensis 13-lipoxygenase 16 in recombinant cells during the conversion of unsaturated fatty acids to hydroxy unsaturated fatty acids were more stable than the purified enzymes. Therefore, instead of purified 8,11-LDS, recombinant cells expressing 8,11-LDS from P. chrysogenum were used for the production of hydroxy fatty acids.…”
Section: Resultsmentioning
confidence: 94%
See 1 more Smart Citation
“…Oxygenases such as A. nidulans 5,8-LDS 10 and Burkholderia thailandensis 13-lipoxygenase 16 in recombinant cells during the conversion of unsaturated fatty acids to hydroxy unsaturated fatty acids were more stable than the purified enzymes. Therefore, instead of purified 8,11-LDS, recombinant cells expressing 8,11-LDS from P. chrysogenum were used for the production of hydroxy fatty acids.…”
Section: Resultsmentioning
confidence: 94%
“…Although orthogonal experiments can be achieved more accurately optimal reaction conditions, the optimization for the production of hydroxy fatty acids has been mainly performed using single factor experiments , . The interactions between pH and temperature and between cell density and substrate concentration were a little (Supporting Information Figure S1).…”
Section: Resultsmentioning
confidence: 99%
“…We used E. coli cells for the biotransformation of PUFAs into THFAs instead of the isolated enzyme because recombinant E. coli has been used for HFA production because whole-cell reactions are more economical and stable than enzymatic reactions. 27,28 For enhanced production of 4 , the reaction conditions, including pH, temperature, and cell and substrate concentrations, were optimized by varying the pH of 7.0 to 9.5, the temperature of 15 to 35 °C, the cell concentration of 10 to 50 g L −1 cells, and the substrate concentration of 50 to 500 mM 1 , respectively (Fig. S11†).…”
Section: Resultsmentioning
confidence: 99%
“…The reaction was performed in 50 mM HEPES (pH 7.0) buffer containing 1 mM ARA and 0.5 g L À1 cells for 20 min. ARA, arachidonic acid; HETE, hydroxyeicosatetraenoic acid; LOX, lipoxygenase Instead of enzymes, cells have been used as an economically viable biocatalyst to produce HFAs because they are more stable than enzymes and do not require enzyme extraction and purification steps (Sim et al, 2015). Moreover, under the optimized conditions of each cell or enzyme, the molar conversion and volumetric productivity of recombinant E. coli cells was significantly higher than those of the purified enzyme (Shin et al, 2019).…”
Section: Resultsmentioning
confidence: 99%