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Over ons Praktische zaken Waar vindt u ons E. (Edita) Jurak, Dr

Research interests

The research done in Dr. Jurak's group (Department of Chemical Engineering, ENTEG) focuses on the biocatalysis and enzyme discovery for modification of complex polymers such as carbohydrates and plastics.

The more fundamental research is directed towards understanding how microbial enzymes work and work together (gene clusters) to modify given polymers. Large focus area is understanding enzyme function, structure and properties, studying natural diversity of enzymes, and getting insights into the changes of the polymer structure and physical properties upon the enzyme’s action.

Examples are 1) the structure-function relationship of GH13 and GH57 microbial glycogen branching enzymes. 2) unravelling the function of uncharacterized enzymes from plant biomass related GH families and proteins of unknown function (PUFs) from bacterial gene clusters through transcriptomic and sequence analysis and in-depth biochemical characterization. 3) biocatalysis of plastic polymers (PVC).

Publicaties

A novel acetyl xylan esterase enabling complete deacetylation of substituted xylans

Occurrence and function of enzymes for lignocellulose degradation in commercial Agaricus bisporus cultivation

Characterization of Two Glycoside Hydrolases of Family GH13 and GH57, Present in a Polysaccharide Utilization Locus (PUL) of Pontibacter sp. SGAir0037

Enrichment of Aquatic Xylan-Degrading Microbial Communities

Impact of GOS and 2’-FL on the production and structural composition of membrane-associated exopolysaccharides by B. adolescentis and B. infantis

Novel β-galactosidase activity and first crystal structure of Glycoside Hydrolase family 154

Polysaccharide utilization loci encoded DUF1735 likely functions as membrane-bound spacer for carbohydrate active enzymes

The production and characteristics of glycogen synthesized by various strains of the thermoacidophilic red microalgae Galdieria grown heterotrophically

Alpha-1,4-transglycosylation Activity of GH57 Glycogen Branching Enzymes Is Higher in the Absence of a Flexible Loop with a Conserved Tyrosine Residue

The Synergistic Effect of GH13 and GH57 GBEs of Petrotoga mobilis Results in α-Glucan Molecules with a Higher Branch Density

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