Primary Structure Analysis and Functional Expression of Erythrose Reductases from Erythritol-Producing Fungi (<i>Trichosporonoides megachiliensis</i>SNG-42)

Ookura, Tetsuya; Azuma, Keiko; Isshiki, Kenji; Taniguchi, Hajime; Kasumi, Takafumi; Kawamura, Yukio

doi:10.1271/bbb.69.944

Cited by 28 publications

(21 citation statements)

References 12 publications

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“…In S. cerevisiae, GPD1 (glyceraldehyde-3-phosphate dehydrogenase gene 1) is well known to modulate osmotic imbalance in the cell when exposed to a hyper-osmotic environment, but GPD2 apparently does not (28). Previously, we obtained similar results with the erythrose reductase (ER) isogenes, ER1, ER2, and ER3, derived from M. megachiliensis, and found that ER3 expression specifically was responsive to osmotic stress caused by glucose (20,29).…”

Section: Discussionsupporting

confidence: 52%

Two transaldolase isogenes from Moniliella megachiliensis behave in a different way depending on the stress class

Iwata

Mizushima

Kobayashi

et al. 2015

Journal of Bioscience and Bioengineering

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Section: Discussionsupporting

confidence: 52%

Two transaldolase isogenes from Moniliella megachiliensis behave in a different way depending on the stress class

Iwata

Mizushima

Kobayashi

et al. 2015

Journal of Bioscience and Bioengineering

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“…Motivated by the fact that mineral supplementation enhances erythritol synthesis by many various microorganisms [21, 44, 45] we set out to determine whether minerals have an effect on YlER activity. The optimum pH of 3.0 as the most favorable condition was selected for analyzing the effects of metal ions on YlER activity.…”

Section: Resultsmentioning

confidence: 99%

“…The final step is catalyzed by erythrose reductase (ER), which reduces erythrose to erythritol with concomitant NAD(P)H oxidation [3, 19]. Several studies have been conducted on ER derived from Candida magnoliae [20], Moniliella megachiliensis ( Trichosporonoides megachiliensis) [21] and Trichoderma reesei [22]. Moreover, it was shown that ER is a crucial gene in erythritol synthesis [4].…”

Section: Introductionmentioning

confidence: 99%

Characterization of erythrose reductase from Yarrowia lipolytica and its influence on erythritol synthesis

et al. 2017

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BackgroundErythritol is a natural sweetener that is used in the food industry. It is produced as an osmoprotectant by bacteria and yeast. Due to its chemical properties, it does not change the insulin level in the blood, and therefore it can be safely used by diabetics. Previously, it has been shown that erythrose reductase (ER), which catalyzes the final step, plays a crucial role in erythritol synthesis. ER reduces erythrose to erythritol with NAD(P)H as a cofactor. Despite many studies on erythritol synthesis by Yarrowia lipolytica, the enzymes involved in this metabolic pathway have ever been described.ResultsThe gene YALI0F18590g encoding the predicted erythrose reductase from Y. lipolytica was overexpressed, and its influence on erythritol synthesis was studied. The amino acid sequence of the Y. lipolytica ER showed a high degree of similarity to the previously described erythrose reductases from known erythritol producers, such as Candida magnoliae and Moniliella megachiliensis. Here, we found that the gene overexpression results in an enhanced titer of erythritol of 44.44 g/L (20% over the control), a yield of 0.44 g/g and productivity of 0.77 g/L/h. Moreover, on purification and characterization of the enzyme we found that it displays the highest activity at 37 °C and pH 3.0. The effects of various metal ions (Zn2+, Cu2+, Mn2+, Fe2+) on erythrose reductase were investigated. The addition of Zn2+ ions at 0.25 mM had a positive effect on the activity of erythrose reductase from Y. lipolytica, as well as on the erythritol production.ConclusionsIn this study we identified, overexpressed and characterized a native erythrose reductase in Y. lipolytica. Further optimizations of this strain via metabolic pathway engineering and media optimization strategies enabled 54 g/L to be produced in a shake-flask experiment. To date, this is the first reported study employing metabolic engineering of the native gene involved in the erythritol pathway to result in a high titer of the polyol. Moreover, it indicates the importance of environmental conditions for genetic targets in metabolic engineering.Electronic supplementary materialThe online version of this article (doi:10.1186/s12934-017-0733-6) contains supplementary material, which is available to authorized users.

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“…Interestingly, N61188-12 gave lower yields of total glycerol and ribitol, which may be the reason why it has such high erythritol production. Recently, the genes of three isozymes of NADPH-dependent erythrose reductases (ER-I, ER-II, and ER-III) in erythritol-producing fungi, Trichosporonoides megachiliensis SNG-42, which catalyze the reduction of D-erythrose, were cloned, expressed in Escherichia coli, and characterized [23]. Moreover, the proteomic information of C. magnoliae has been applied to predict the carbon metabolism of erythritol-synthesizing microorganisms, at the gene level [15,16].…”

Section: Discussionmentioning

confidence: 99%

High-level production of erythritol by mutants of osmophilic Moniliella sp.

Lin

Wen

Wang

et al. 2010

Process Biochemistry

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Primary Structure Analysis and Functional Expression of Erythrose Reductases from Erythritol-Producing Fungi (Trichosporonoides megachiliensisSNG-42)

Cited by 28 publications

References 12 publications

Two transaldolase isogenes from Moniliella megachiliensis behave in a different way depending on the stress class

Two transaldolase isogenes from Moniliella megachiliensis behave in a different way depending on the stress class

Characterization of erythrose reductase from Yarrowia lipolytica and its influence on erythritol synthesis

High-level production of erythritol by mutants of osmophilic Moniliella sp.

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