References of "Vandermies, Marie"
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See detailEYK1 encoding erythrulose kinase as a catabolic selectable marker for genome editing in the non-conventional yeast Yarrowia lipolytica
Vandermies, Marie ULg; Denies, Olivia ULg; Nicaud, Jean-Marc et al

in Journal of Microbiological Methods (2017), 139

We report here on EYK1, encoding erythrulose kinase, as an efficient catabolic selectable marker for genome editing in Y. lipolytica. Compared to auxotrophic markers, EYK1 increases the growth rate of ... [more ▼]

We report here on EYK1, encoding erythrulose kinase, as an efficient catabolic selectable marker for genome editing in Y. lipolytica. Compared to auxotrophic markers, EYK1 increases the growth rate of transformants and allows improved efficiency of transformation. The utility of the marker EYK1 in a replicative vector was also demonstrated. [less ▲]

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See detailEnhancing erythritol productivity in Yarrowia lipolytica using metabolic engineering
Carly, Frédéric; Vandermies, Marie ULg; Telek, Samuel ULg et al

in Metabolic Engineering (2017), 42

Erythritol (1,2,3,4-butanetetrol) is a four-carbon sugar alcohol with sweetening properties that is used by the agrofood industry as a food additive. In this study, we demonstrated that metabolic ... [more ▼]

Erythritol (1,2,3,4-butanetetrol) is a four-carbon sugar alcohol with sweetening properties that is used by the agrofood industry as a food additive. In this study, we demonstrated that metabolic engineering can be used to improve the production of erythritol from glycerol in the yeast Yarrowia lipolytica. The best results were obtained using a mutant that overexpressed GUT1 and TKL1, which encode a glycerol kinase and a transketolase, respectively, and in which EYK1, which encodes erythrulose kinase, was disrupted; the latter enzyme is involved in an early step of erythritol catabolism. In this strain, erythritol productivity was 75% higher than in the wild type; furthermore, the culturing time needed to achieve maximum concentration was reduced by 40%. An additional advantage is that the strain was unable to consume the erythritol it had created, further increasing the process's efficiency. The erythritol productivity values we obtained here are among the highest reported thus far. [less ▲]

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See detailDiscovering novel enzymes y functional screening of plurigenomic libraries from alga-associated Flavobacteriia and Gammaproteobacteria
Martin, Marjolaine ULg; Vandermies, Marie ULg; Joyeux, Coline et al

in Microbiological Research (2016), 186

Alga-associated microorganisms, in the context of their numerous interactions with the host and thecomplexity of the marine environment, are known to produce diverse hydrolytic enzymes with ... [more ▼]

Alga-associated microorganisms, in the context of their numerous interactions with the host and thecomplexity of the marine environment, are known to produce diverse hydrolytic enzymes with originalbiochemistry. We recently isolated several macroalgal-polysaccharide-degrading bacteria from the sur-face of the brown alga Ascophyllum nodosum. These active isolates belong to two classes: the Flavobacteriiaand the Gammaproteobacteria. In the present study, we constructed two “plurigenomic” (with multi-ple bacterial genomes) libraries with the 5 most interesting isolates (regarding their phylogeny andtheir enzymatic activities) of each class (Fv and Gm libraries). Both libraries were screened for diversehydrolytic activities. Five activities, out of the 48 previously identified in the natural polysaccharolyticisolates, were recovered by functional screening: a xylanase (GmXyl7), a beta-glucosidase (GmBg1), anesterase (GmEst7) and two iota-carrageenases (Fvi2.5 and Gmi1.3). We discuss here the potential role ofthe used host-cell, the average DNA insert-sizes and the used restriction enzymes on the divergent screen-ing yields obtained for both libraries and get deeper inside the “great screen anomaly”. Interestingly, thediscovered esterase probably stands for a novel family of homoserine o-acetyltransferase-like-esterases,while the two iota-carrageenases represent new members of the poorly known GH82 family (contain-ing only 19 proteins since its description in 2000). These original results demonstrate the efficiencyof our uncommon “plurigenomic” library approach and the underexplored potential of alga-associatedcultivable microbiota for the identification of novel and algal-specific enzymes. [less ▲]

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