0000000000994717

AUTHOR

Nadiya Shevchuk

showing 3 related works from this author

Additional file 2 of Engineering of sugar transporters for improvement of xylose utilization during high-temperature alcoholic fermentation in Ogatae…

2020

Additional file 2: Table S1. List of primers used in this study.

researchProduct

Engineering of sugar transporters for improvement of xylose utilization during high-temperature alcoholic fermentation in Ogataea polymorpha yeast

2020

Abstract Background Xylose transport is one of the bottlenecks in the conversion of lignocellulosic biomass to ethanol. Xylose consumption by the wild-type strains of xylose-utilizing yeasts occurs once glucose is depleted resulting in a long fermentation process and overall slow and incomplete conversion of sugars liberated from lignocellulosic hydrolysates. Therefore, the engineering of endogenous transporters for the facilitation of glucose-xylose co-consumption is an important prerequisite for efficient ethanol production from lignocellulosic hydrolysates. Results In this study, several engineering approaches formerly used for the low-affinity glucose transporters in Saccharomyces cerev…

Hot TemperatureXylose transportersSaccharomyces cerevisiaelcsh:QR1-502Lignocellulosic biomassBioengineeringEthanol fermentationXyloseProtein EngineeringApplied Microbiology and BiotechnologyPichialcsh:MicrobiologyFungal Proteinschemistry.chemical_compoundHigh-temperature alcoholic fermentationOgataea (Hansenula) polymorphaEthanol fuelXylosebiologyChemistryResearchbiology.organism_classificationYeastBiochemistryAlcoholsFermentationFermentationOgataea polymorphaBiotechnology
researchProduct

Additional file 1 of Engineering of sugar transporters for improvement of xylose utilization during high-temperature alcoholic fermentation in Ogatae…

2020

Additional file 1: Figure S1. Alignment of amino acid sequences of O. polymorpha Hxt1 and S. cerevisiae Hxt1, Hxt3, Hxt6, Hxt7 transporters. Figure S2. Sequence of O. polymorpha Hxt1 transporter. The lysine residues substituted for arginine are shaded grey. The position of the asparagine residue that was mutated to an alanine to obtain Hxt1-N358A mutant is underlined. Figure S3. Linear schemes of plasmids for overexpression of the modified versions of Hxt1, Gal2 and Hxt7 transporters.

researchProduct