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D-Xylose Metabolism by Mutant Strains of Candida sp
1983The first step in the metabolism of d-xylose by yeasts and mycelial fungi was found to be the reduction of d-xylose to xylitol, a reaction catalyzed by NADPH-linked d-xylose reductase. This step is followed by the oxidation of xylitol to d-xylulose which is catalyzed by NAD-linked xylitol dehydrogenase.
L D, McCracken, C S, Gong
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Metabolism of d-xylose in Schizosaccharomyces pombe cloned with a xylose isomerase gene
Applied Microbiology and Biotechnology, 1989The Escherichia coli xylose isomerase gene was transformed into Schizosaccharomyces pombe for direct d-xylose utilization. In order to understand d-xylose metabolism and determine the limiting factors on d-xylose utilization by the transformed yeast, d-xylose transport, xylose isomerization, and xylulose phosphorylation were investigated.
Err-Cheng Chan +2 more
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Calculation of metabolic flow of xylose in Lactococcus lactis
Journal of Bioscience and Bioengineering, 2007A circuit diagram is proposed on the basis of an analysis of metabolic pathways of lactic acid bacteria, namely, a phosphoketolase pathway and a pentose phosphate/glycolic pathway. An augmented matrix was derived from carbon balances and stoichiometries from the circuit diagram, and solved by Gaussian elimination.
Hitomi, Ohara +2 more
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Strain engineering of Saccharomyces cerevisiae for enhanced xylose metabolism
Biotechnology Advances, 2013Efficient and rapid fermentation of all sugars present in cellulosic hydrolysates is essential for economic conversion of renewable biomass into fuels and chemicals. Xylose is one of the most abundant sugars in cellulosic biomass but it cannot be utilized by wild type Saccharomyces cerevisiae, which has been used for industrial ethanol production ...
Soo Rin, Kim +3 more
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Xylose metabolism in Pachysolen tannophilus: purification and properties of xylose reductase
Canadian Journal of Microbiology, 1984Xylose reductase (xylitol: NADP oxidoreductase, EC 1.1.1.139) has been purified from D-xylose grown cells of the yeast Pachysolen tannophilus by application of DEAE-cellulose ion exchange chromatography, 2′,5′-ADP-Sepharose affinity chromatography, Biogel P200 gel filtration, and dextran blue Sepharose chromatography to approximately 95% homogeneity ...
Günther Ditzelmüller +3 more
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Xylose metabolism by Candida shehatae in continuous culture
Applied Microbiology and Biotechnology, 1988Xylose metabolism by Candida shehatae in continuous culture was examined under both fully-aerobic and semi-aerobic conditions. Growth did not occur in the absence of respiration. Under fully-aerobic conditions, the cell yield was constant at 0.51 g/g and the specific respiration rate Qo2was linearly related to the specific growth rate μ with a slope of
M. A. Alexander +2 more
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World Journal of Microbiology & Biotechnology, 2022
Viviani Tadioto +13 more
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Viviani Tadioto +13 more
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Applied Microbiology and Biotechnology, 2009
During growth of Saccharomyces cerevisiae on glucose, the redox cofactors NADH and NADPH are predominantly involved in catabolism and biosynthesis, respectively. A deviation from the optimal level of these cofactors often results in major changes in the substrate uptake and biomass formation.
Jin, Hou +3 more
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During growth of Saccharomyces cerevisiae on glucose, the redox cofactors NADH and NADPH are predominantly involved in catabolism and biosynthesis, respectively. A deviation from the optimal level of these cofactors often results in major changes in the substrate uptake and biomass formation.
Jin, Hou +3 more
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Xylose Metabolism in Bioethanol Production: Saccharomyces cerevisiae vs Non-Saccharomyces Yeasts
Bioenergy Research, 2021Alfayuset Ochoa-Chacón +5 more
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Chemico-Biological Interactions, 2001
The primary structure of the aldose xylose reductase from Candida tenuis (CtAR) is shown to be 39% identical to that of human aldose reductase (hAR). The catalytic tetrad of hAR is completely conserved in CtAR (Tyr51, Lys80, Asp46, His113). The amino acid residues involved in binding of NADPH by hAR (D.K.
B, Nidetzky +3 more
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The primary structure of the aldose xylose reductase from Candida tenuis (CtAR) is shown to be 39% identical to that of human aldose reductase (hAR). The catalytic tetrad of hAR is completely conserved in CtAR (Tyr51, Lys80, Asp46, His113). The amino acid residues involved in binding of NADPH by hAR (D.K.
B, Nidetzky +3 more
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