Metabolic Engineering of
            <i>Saccharomyces cerevisiae</i>

Østergaard, Simon; Olsson, Lisbeth; Nielsen, Jens

doi:10.1128/mmbr.64.1.34-50.2000

Cited by 400 publications

(217 citation statements)

References 154 publications

(132 reference statements)

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“…Sucrose was hydrolyzed extracellularly by the action of S. cerevisiae invertase producing equimolar glucose and fructose initially 1,14 , which was then utilized by the yeast. Therefore, the longest lag time of ethanol production observed on sucrose was understandable in this case.…”

Section: Figmentioning

confidence: 99%

Fermentation Kinetics of Different Sugars by Apple Wine YeastSaccharomyces cerevisiae

Wang

et al. 2004

Journal of the Institute of Brewing

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A non-linear kinetic model to predict the consumption of different sugars (glucose, fructose and sucrose) as a substrate, during an apple wine yeast fermentation with Saccharomyces cerevisiae strain CCTCC M201022 is proposed. This model was used to predict sugar utilization by this yeast beginning at various initial sugar concentrations. After observation of the experimental data, a model based on the logistic equation of yeast growth, growthassociated production of ethanol with a lag time, and consumption of sugars for biomass formation and maintenance, was developed. After experimental model fitting, kinetic parameters in the model were estimated. The experimental verification of the model was performed using flask-scale fermentations, and the model obtained predicted the fermentation performance effectively, using different sugars as the substrate set at various initial sugar concentrations. Based on estimated kinetic parameters and the characteristics of sugar utilization, the yeast examined appeared to be glucophilic. The effects of different sugars with various initial concentrations on the fermentation performance by this yeast were investigated, and some applications of kinetic parameters are discussed.

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Section: Figmentioning

confidence: 99%

Fermentation Kinetics of Different Sugars by Apple Wine YeastSaccharomyces cerevisiae

Wang

et al. 2004

Journal of the Institute of Brewing

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“…An efficient, high-flux pathway should recycle the co-substrate such that there is no net conversion of NADPH into NADH resulting from xylose metabolism. Perturbations in this ratio have been linked to cellular stress and xylitol excretion [9]. An XR that is exclusively specific for NADH could alleviate this problem.…”

Section: Introductionmentioning

confidence: 99%

Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases

Kavanagh

Klimacek

Nidetzky

et al. 2003

Biochemical Journal

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Xylose reductase (XR; AKR2B5) is an unusual member of aldoketo reductase superfamily, because it is one of the few able to efficiently utilize both NADPH and NADH as co-substrates in converting xylose into xylitol. In order to better understand the basis for this dual specificity, we have determined the crystal structure of XR from the yeast Candida tenuis in complex with NAD + to 1.80 Å resolution (where 1 Å = 0.1 nm) with a crystallographic R-factor of 18.3 %. A comparison of the NAD + -and the previously determined NADP + -bound forms of XR reveals that XR has the ability to change the conformation of two loops. To accommodate both the presence and absence of the 2 -phosphate, the enzyme is able to adopt different conformations for several different side chains on these loops, including Asn 276 , which makes alternative hydrogen-bonding interactions with the adenosine ribose. Also critical is the presence of Glu 227 on a short rigid helix, which makes hydrogen bonds to both the 2 -and 3 -hydroxy groups of the adenosine ribose. In addition to changes in hydrogen-bonding of the adenosine, the ribose unmistakably adopts a 3 -endo conformation rather than the 2 -endo conformation seen in the NADP + -bound form. These results underscore the importance of tight adenosine binding for efficient use of either NADH or NADPH as a co-substrate in aldo-keto reductases. The dual specificity found in XR is also an important consideration in designing a high-flux xylose metabolic pathway, which may be improved with an enzyme specific for NADH.

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“…Pentose fermentation in industrial strains of S. cerevisiae such as TMB 3006, TMB 3400 and 424A (LNF-ST), containing heterologous xylose reductase and xylitol dehydrogenase, achieved yields of over 0.4 g ethanol per g sugar (Hahn-Hä gerdal et al, 2007). S. cerevisiae metabolic engineering is still a topic of great interest, and a number of excellent reviews have addressed this specific topic (Ho et al, 2000;Jeffries and Jin, 2004;Ostergaard et al, 2000). Metabolic pathway engineering may also improve the ethanol production of some native xylose-metabolizing yeasts such as P. stipitis, Pichia segobiensis, Candida sheatae and Pachysolen tannophilus, although the metabolic potential of these yeasts is still poorly understood (Jeffries, 2006).…”

Section: Ethanol (Ch 3 Ch 2 Oh; C 2 H 6 O)mentioning

confidence: 99%

Microbial conversion of sugars from plant biomass to lactic acid or ethanol

2008

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SummaryConcerns for our environment and unease with our dependence on foreign oil have renewed interest in converting plant biomass into fuels and 'green' chemicals. The volume of plant matter available makes lignocellulose conversion desirable, although no single isolated organism has been shown to depolymerize lignocellulose and efficiently metabolize the resulting sugars into a specific product. This work reviews selected chemicals and fuels that can be produced from microbial fermentation of plant-derived cell-wall sugars and directed engineering for improvement of microbial biocatalysts. Lactic acid and ethanol production are highlighted, with a focus on engineered Escherichia coli.

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Metabolic Engineering of Saccharomyces cerevisiae

Cited by 400 publications

References 154 publications

Fermentation Kinetics of Different Sugars by Apple Wine YeastSaccharomyces cerevisiae

Fermentation Kinetics of Different Sugars by Apple Wine YeastSaccharomyces cerevisiae

Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases

Microbial conversion of sugars from plant biomass to lactic acid or ethanol

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