Results 171 to 180 of about 127,929 (201)
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Process Biochemistry, 2020
Abstract The co-production of xylitol and ethanol from agricultural straw has more economic advantages than the production of ethanol only. Saccharomyces cerevisiae, the most widely used ethanol-producing yeast, can be genetically engineered to ferment xylose to xylitol.
Bai-Xue Yang +5 more
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Abstract The co-production of xylitol and ethanol from agricultural straw has more economic advantages than the production of ethanol only. Saccharomyces cerevisiae, the most widely used ethanol-producing yeast, can be genetically engineered to ferment xylose to xylitol.
Bai-Xue Yang +5 more
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The Production and Properties of a New Xylose Reductase from Fungus Neurospora crassa
Applied Biochemistry and Biotechnology, 1998Neurospora crassa XI was found to ferment xylose and glucose simultaneously. Xylose was the appropriate inducer for the production of xylose reductase that had two isoenzymes designated as EI and EII. Both EI and EII, which were purified by affinity chromatography, had NADPH-dependent xylose reductase activities.
X, Zhao, P, Gao, Z, Wang
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Applied Biochemistry and Biotechnology, 2003
We changed the fluxes of xylose metabolites in recombinant Saccharomyces cerevisiae by manipulating expression of Pichia stipitis genes (XYL1 and XYL2) coding for xylose reductase (XR) and xylitol dehydrogenase (XDH), respectively. XYL1 copy number was kept constant by integrating it into the chromosome.
Yong-Su, Jin, Thomas W, Jeffries
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We changed the fluxes of xylose metabolites in recombinant Saccharomyces cerevisiae by manipulating expression of Pichia stipitis genes (XYL1 and XYL2) coding for xylose reductase (XR) and xylitol dehydrogenase (XDH), respectively. XYL1 copy number was kept constant by integrating it into the chromosome.
Yong-Su, Jin, Thomas W, Jeffries
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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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NADPH-dependent D-aldose reductases and xylose fermentation in Fusarium oxysporum
Journal of Bioscience and Bioengineering, 2004Two aldose (xylose) reductases (ARI and ARII) from Fusarium oxysporum were purified and characterized. The native ARI was a monomer with M(r) 41000, pI 5.2 and showed a 52-fold preference for NADPH over NADH, while ARII was homodimeric with a subunit of M(r) 37000, pI 3.6 and a 60-fold preference for NADPH over NADH.
Christakopoulos, P, Panagiotou, G
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Induction of Xylose Reductase in Germinating Spores of Penicillium Chrysogenum
Mycologia, 1962In an investigation of the metabolism of D-xylose by cell-free extracts of Penicillium chrysogenum Thom, Chiang and Knight (1959) stated that the soluble TPNH-linked enzyme which catalyzes the reduction of xylose to xylitol, and for which they proposed the name D-xylose reductase ". . . appears to be inducible . .
Joseph M. Kornfeld, S. G. Knight
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Review: The structure and function of yeast xylose (aldose) reductases
Yeast, 1998Yeast xylose (aldose) reductases are members of the aldo-keto reductase family of enzymes which are widely distributed in a variety of other organisms. In yeasts, these enzymes catalyse the first step of xylose metabolism where xylose is converted to xylitol.
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Use of xylose reductase as a cofactor enhancing system for in vivo biocatalysis
Cofactor imbalance is a common challenge in whole-cell bioconversion and thus limits the efficiency of biocatalysts. Various approaches have been employed to enhance cofactor availability, including specific engineering of pathways to increase intracellular levels of NAD(P)H, FMN, FAD, ATP and CoA. Recently, we have demonstrated that addition of xyloseChalermroj, Sutthaphirom +1 more
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Characterization of -xylose reductase, XyrB, from
Biotechnology Reports (Amsterdam, Netherlands), 2021Maria Victoria Aguilar-Pontes +2 more
exaly