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Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate.
Appl Environ Microbiol. 2001 Sep; 67(9):4249-55.AE

Abstract

Fermentation of the pentose sugar xylose to ethanol in lignocellulosic biomass would make bioethanol production economically more competitive. Saccharomyces cerevisiae, an efficient ethanol producer, can utilize xylose only when expressing the heterologous genes XYL1 (xylose reductase) and XYL2 (xylitol dehydrogenase). Xylose reductase and xylitol dehydrogenase convert xylose to its isomer xylulose. The gene XKS1 encodes the xylulose-phosphorylating enzyme xylulokinase. In this study, we determined the effect of XKS1 overexpression on two different S. cerevisiae host strains, H158 and CEN.PK, also expressing XYL1 and XYL2. H158 has been previously used as a host strain for the construction of recombinant xylose-utilizing S. cerevisiae strains. CEN.PK is a new strain specifically developed to serve as a host strain for the development of metabolic engineering strategies. Fermentation was carried out in defined and complex media containing a hexose and pentose sugar mixture or a birch wood lignocellulosic hydrolysate. XKS1 overexpression increased the ethanol yield by a factor of 2 and reduced the xylitol yield by 70 to 100% and the final acetate concentrations by 50 to 100%. However, XKS1 overexpression reduced the total xylose consumption by half for CEN.PK and to as little as one-fifth for H158. Yeast extract and peptone partly restored sugar consumption in hydrolysate medium. CEN.PK consumed more xylose but produced more xylitol than H158 and thus gave lower ethanol yields on consumed xylose. The results demonstrate that strain background and modulation of XKS1 expression are important for generating an efficient xylose-fermenting recombinant strain of S. cerevisiae.

Authors+Show Affiliations

Department of Applied Microbiology, Lund University, 221 00 Lund, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11526030

Citation

Johansson, B, et al. "Xylulokinase Overexpression in Two Strains of Saccharomyces Cerevisiae Also Expressing Xylose Reductase and Xylitol Dehydrogenase and Its Effect On Fermentation of Xylose and Lignocellulosic Hydrolysate." Applied and Environmental Microbiology, vol. 67, no. 9, 2001, pp. 4249-55.
Johansson B, Christensson C, Hobley T, et al. Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate. Appl Environ Microbiol. 2001;67(9):4249-55.
Johansson, B., Christensson, C., Hobley, T., & Hahn-Hägerdal, B. (2001). Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate. Applied and Environmental Microbiology, 67(9), 4249-55.
Johansson B, et al. Xylulokinase Overexpression in Two Strains of Saccharomyces Cerevisiae Also Expressing Xylose Reductase and Xylitol Dehydrogenase and Its Effect On Fermentation of Xylose and Lignocellulosic Hydrolysate. Appl Environ Microbiol. 2001;67(9):4249-55. PubMed PMID: 11526030.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate. AU - Johansson,B, AU - Christensson,C, AU - Hobley,T, AU - Hahn-Hägerdal,B, PY - 2001/8/30/pubmed PY - 2002/1/5/medline PY - 2001/8/30/entrez SP - 4249 EP - 55 JF - Applied and environmental microbiology JO - Appl Environ Microbiol VL - 67 IS - 9 N2 - Fermentation of the pentose sugar xylose to ethanol in lignocellulosic biomass would make bioethanol production economically more competitive. Saccharomyces cerevisiae, an efficient ethanol producer, can utilize xylose only when expressing the heterologous genes XYL1 (xylose reductase) and XYL2 (xylitol dehydrogenase). Xylose reductase and xylitol dehydrogenase convert xylose to its isomer xylulose. The gene XKS1 encodes the xylulose-phosphorylating enzyme xylulokinase. In this study, we determined the effect of XKS1 overexpression on two different S. cerevisiae host strains, H158 and CEN.PK, also expressing XYL1 and XYL2. H158 has been previously used as a host strain for the construction of recombinant xylose-utilizing S. cerevisiae strains. CEN.PK is a new strain specifically developed to serve as a host strain for the development of metabolic engineering strategies. Fermentation was carried out in defined and complex media containing a hexose and pentose sugar mixture or a birch wood lignocellulosic hydrolysate. XKS1 overexpression increased the ethanol yield by a factor of 2 and reduced the xylitol yield by 70 to 100% and the final acetate concentrations by 50 to 100%. However, XKS1 overexpression reduced the total xylose consumption by half for CEN.PK and to as little as one-fifth for H158. Yeast extract and peptone partly restored sugar consumption in hydrolysate medium. CEN.PK consumed more xylose but produced more xylitol than H158 and thus gave lower ethanol yields on consumed xylose. The results demonstrate that strain background and modulation of XKS1 expression are important for generating an efficient xylose-fermenting recombinant strain of S. cerevisiae. SN - 0099-2240 UR - https://www.unboundmedicine.com/medline/citation/11526030/Xylulokinase_overexpression_in_two_strains_of_Saccharomyces_cerevisiae_also_expressing_xylose_reductase_and_xylitol_dehydrogenase_and_its_effect_on_fermentation_of_xylose_and_lignocellulosic_hydrolysate_ L2 - https://journals.asm.org/doi/10.1128/AEM.67.9.4249-4255.2001?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -