Purification and properties of the NAD+-xylitol-dehydrogenase from the yeast Pichia stipitis

Rizzi, Manfred; Harwart, Katharina; Erlemann, Petra; Bui-Thanh, Ngoc-Anh; Dellweg, H.

doi:10.1016/0922-338x(89)90080-9

Cited by 119 publications

(77 citation statements)

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“…However, in these strains a major product has been xylitol, caused by a co-factor imbalance between the NAD(P)H consuming XR (Rizzi et al, 1988) and the NADH forming XDH (Rizzi et al, 1989) reactions (Bruinenberg et al, 1983;Kötter and Ciriacy, 1993). The xylose consumption rate is also lower than the glucose consumption rate, and besides the co-factor imbalance this has been attributed to too low levels of enzymes in the pentose phosphate pathway (PPP) (Senac and Hahn-Hägerdal, 1990) and to limitations in transport (Meinander et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

“…Gre3p has been purified and it is strictly NADPH dependent (Kuhn et al, 1995;Ford and Ellis, 2001;Jeong et al, 2001;Petrash et al, 2001), in contrast to XR from P. stipitis, which uses both NADH and NADPH (Rizzi et al, 1989), and the kinetic properties of Gre3p have been characterized. The K m for xylose suggests that this protein is a xylose reductase with the ability to reduce several other compounds, including arabinose, glyceraldehydes, methylglyoxal and β-keto esters (Kuhn et al, 1995;Rodríguez et al, 2000;Ford and Ellis, 2001;Petrash et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

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Endogenous NADPH‐dependent aldose reductase activity influences product formation during xylose consumption in recombinant Saccharomyces cerevisiae

Bjerre

Jeppsson

Hahn‐Hägerdal

et al. 2003

Yeast

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Introduction of the xylose pathway from Pichia stipitis into Saccharomyces cerevisiae enables xylose utilization in recombinant S. cerevisiae. However, xylitol is a major by-product. An endogenous aldo-keto reductase, encoded by the GRE3 gene, was expressed at different levels in recombinant S. cerevisiae strains to investigate its effect on xylose utilization. In a recombinant S. cerevisiae strain producing only xylitol dehydrogenase (XDH) from P. stipitis and an extra copy of the endogenous xylulokinase (XK), ethanol formation from xylose was mediated by Gre3p, capable of reducing xylose to xylitol. When the GRE3 gene was overexpressed in this strain, the xylose consumption and ethanol formation increased by 29% and 116%, respectively. When the GRE3 gene was deleted in the recombinant xylose-fermenting S. cerevisiae strain TMB3001 (which possesses xylose reductase and XDH from P. stipitis, and an extra copy of endogenous XK), the xylitol yield decreased by 49% and the ethanol yield increased by 19% in anaerobic continuous culture with a glucose/xylose mixture. Biomass was reduced by 31% in strains where GRE3 was deleted, suggesting that fine-tuning of GRE3 expression is the preferred choice rather than deletion.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Endogenous NADPH‐dependent aldose reductase activity influences product formation during xylose consumption in recombinant Saccharomyces cerevisiae

Bjerre

Jeppsson

Hahn‐Hägerdal

et al. 2003

Yeast

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“…This is in good agreement with the predicted molecular mass of 40.8 kDa (39.3-kDa XDH with a 1.5-kDa His-tag). The XDHs from other yeast and fungal strains have similar molecular masses, i.e., 38-41 kDa (10)(11)(12)(13)27).…”

Section: Methodsmentioning

confidence: 99%

Molecular Cloning and Characterization of NAD⁺‐Dependent Xylitol Dehydrogenase from Candida tropicalis ATCC 20913

Kim

2006

Biotechnology Progress

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Induction of xylitol dehydrogenase of Candida tropicalis ATCC 20913 by various carbon sources was investigated. The enzyme activity was induced when the yeast was grown on l‐arabinose and d‐xylose. A novel gene encoding the enzyme was cloned and characterized. The 1,095‐bp coding sequence of the gene encodes a polypeptide of 364 amino acids, with a molecular mass of 39.4 kDa. Sequence analysis of the putative protein showed it to be a member of the zinc‐containing alcohol dehydrogenase family and to have homology to xylitol dehydrogenase genes from other yeasts and fungi. The recombinant xylitol dehydrogenase expressed in Escherichia coli oxidized polyols such as xylitol and d‐sorbitol and reduced ketoses such as d‐xylulose and d‐fructose. It required exclusively NAD or NADH as a cofactor.

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“…Therefore, there has been an www.scienceasia.org attempt to construct recombinants S. cerevisiae strain capable of fermenting xylose by overexpressing the genes encoding enzymes in the xylose fermentation pathway of S. stipitis strain 4,14,15 . Three key step enzymes in S. stipitis xylose fermentation pathway are (1) xylose reductase (EC.1.1.1.21), which converts xylose to xylitol using NAD(P)H as a cofactor 16,17 (2) xylitol dehydrogenase (EC.1.1.1.9), which converts xylitol to xylulose using NAD as a cofactor 18 , and (3) xylulose kinase (EC 2.7.1.17), which converts xylulose to xylulose-5-phosphate 19 . Because under oxygen-limit condition which S. cerevisiae ferments glucose to ethanol, NAD becomes its limiting factor 15 .…”

Section: Introductionmentioning

confidence: 99%

Characterization of xylose-utilizing yeasts isolated from herbivore faeces in Thailand

Lorliam¹,

Akaracharanya²,

Jindamorakot³

et al. 2013

ScienceAsia

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A total of 39 xylose-utilizing yeast strains were isolated from herbivore faeces in Thailand. They were identified as Candida tropicalis (32 isolates), Candida albicans (1 isolate), Pichia terricola (1 isolate), Trichosporon mycotoxinivorans (2 isolates), Sporopachydermia lactativora (2 isolates) and Zygoascus meyerae (1 isolate) based on their morphological, cultural, physiological and biochemical characteristics including the sequence analysis of the D1/D2 region of the large-subunit ribosomal DNA. Thirty seven isolates could ferment xylose to ethanol. Zygoascus meyerae E23 isolated from elephant faeces produced the highest ethanol concentration (3.61 g/l after 72 h). C. tropicalis A26 isolated from cow faeces produced the highest xylitol concentration (43.79 g/l) which corresponded to 0.71 g xylitol/g xylose after 24 h. C. tropicalis A26 xylose reductase showed 98.4% identity and 99.0% similarity to C. tropicalis (ABX60132C) xylose reductase, and showed the tetra-amino acid motif (Ile-Pro-Lys-Ser) which is conserved among NADPH-dependent xylose reductase.

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Purification and properties of the NAD+-xylitol-dehydrogenase from the yeast Pichia stipitis

Cited by 119 publications

References 12 publications

Endogenous NADPH‐dependent aldose reductase activity influences product formation during xylose consumption in recombinant Saccharomyces cerevisiae

Endogenous NADPH‐dependent aldose reductase activity influences product formation during xylose consumption in recombinant Saccharomyces cerevisiae

Molecular Cloning and Characterization of NAD⁺‐Dependent Xylitol Dehydrogenase from Candida tropicalis ATCC 20913

Characterization of xylose-utilizing yeasts isolated from herbivore faeces in Thailand

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Purification and properties of the NAD+-xylitol-dehydrogenase from the yeast Pichia stipitis

Cited by 119 publications

References 12 publications

Endogenous NADPH‐dependent aldose reductase activity influences product formation during xylose consumption in recombinant Saccharomyces cerevisiae

Endogenous NADPH‐dependent aldose reductase activity influences product formation during xylose consumption in recombinant Saccharomyces cerevisiae

Molecular Cloning and Characterization of NAD+‐Dependent Xylitol Dehydrogenase from Candida tropicalis ATCC 20913

Characterization of xylose-utilizing yeasts isolated from herbivore faeces in Thailand

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Molecular Cloning and Characterization of NAD⁺‐Dependent Xylitol Dehydrogenase from Candida tropicalis ATCC 20913