B
Bärbel Hahn-Hägerdal
Researcher at Lund University
Publications - 272
Citations - 27781
Bärbel Hahn-Hägerdal is an academic researcher from Lund University. The author has contributed to research in topics: Xylose & Fermentation. The author has an hindex of 83, co-authored 271 publications receiving 26753 citations. Previous affiliations of Bärbel Hahn-Hägerdal include Stellenbosch University & Technical University of Denmark.
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Journal ArticleDOI
The level of glucose-6-phosphate dehydrogenase activity strongly influences xylose fermentation and inhibitor sensitivity in recombinant Saccharomyces cerevisiae strains.
Marie Jeppsson,Björn Johansson,Peter Ruhdal Jensen,Bärbel Hahn-Hägerdal,Marie F. Gorwa-Grauslund +4 more
TL;DR: Strains with low G6PDH‐activity grew slower in a lignocellulose hydrolysate than the strain with wild‐type G6 PDH‐ activity, which suggested that the availability of intracellular NADPH correlated with tolerance towards lignosine‐derived inhibitors.
Journal ArticleDOI
Control of xylose consumption by xylose transport in recombinant Saccharomyces cerevisiae
Márk Gárdonyi,Marie Jeppsson,Gunnar Lidén,Marie-Francoise Gorwa-Grauslund,Bärbel Hahn-Hägerdal +4 more
TL;DR: This work investigated the control exercised by the transport over the specific xylose utilization rate in two recombinant S. cerevisiae strains, one with low XR activity, TMB3001, and one with high XRActivity,TMB3260, grown in aerobic sugar-limited chemostat.
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Influence of cosubstrate concentration on xylose conversion by recombinant, XYL1-expressing Saccharomyces cerevisiae: a comparison of different sugars and ethanol as cosubstrates.
TL;DR: The differences in xylitol yield observed between some of the other sugars may also reflect differences in redox metabolism, which was suggested to enhance the availability of reduced cofactors for xylose reduction with galactose.
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Identification of an NADH-dependent 5-hydroxymethylfurfural-reducing alcohol dehydrogenase in Saccharomyces cerevisiae.
Boaz Laadan,João R. M. Almeida,Peter Rådström,Bärbel Hahn-Hägerdal,Marie-Francoise Gorwa-Grauslund +4 more
TL;DR: The amino acid sequence revealed three novel mutations that were all predicted at the vicinity of the substrate binding site, which could explain the unusual substrate specificity of the S. cerevisiae HMF alcohol dehydrogenase Adh6.
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Increased Ethanol Productivity in Xylose-Utilizing Saccharomyces cerevisiae via a Randomly Mutagenized Xylose Reductase
TL;DR: A novel approach to improve XR for ethanol production in S. cerevisiae was described, and the improved traits of TMB 3420 were readily transferred to the parent strain by reverse engineering of the mutated XR gene.