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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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The xylose reductase/xylitol dehydrogenase/xylulokinase ratio affects product formation in recombinant xylose-utilising Saccharomyces cerevisiae

TL;DR: Overexpression of XK was found to be necessary for ethanol formation from xylose, and TMB 3004, which was the strain with a XR/XDH/XK ratio corresponding to the theoretical optimal ratio, fermented xyloses to ethanol most efficiently.
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Effect of enhanced xylose reductase activity on xylose consumption and product distribution in xylose-fermenting recombinant Saccharomyces cerevisiae.

TL;DR: The xylose reductase (XR) activity was increased 4-19 times in both TMB3001 and the ZWF1-disrupted strain TMB3255, and the increase in XR activity fully restored the xylOSE consumption rate.
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Ethanolic fermentation of pentoses in lignocellulose hydrolysates.

TL;DR: Different strategies involving strain adaptation, and protein and genetic engineering adopted to overcome different obstacles in the fermentation of lignocellulose hydrolysate, are discussed.
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Enhanced sensitivity in PCR detection of Listeria monocytogenes in soft cheese through use of an aqueous two-phase system as a sample preparation method.

TL;DR: The results suggest that the improved detection sensitivity following partitioning of the cheese homogenate in an aqueous two-phase system may be due to partitioned of the PCR inhibitors to the polyethylene glycol phase.
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Reagentless chemically modified carbon paste electrode based on a phenothiazine polymer derivative and yeast alcohol dehydrogenase for the analysis of ethanol

TL;DR: In this paper, an amperometric biosensors for ethanol were constructed by immobilizing yeast alcohol dehydrogenase (ADH) on carbon paste (graphite powder: paraffin oil) chemically modified with a polymer to which a necessary mediator for electrocatalytic NADH oxidation had been covalently attached.