dr hab. KATARZYNA HUPERT-KOCUREK

adiunkt
Kierownik Studiów Doktoranckich

Jagiellońska 28, 40-032 Katowice
pokój nr: C 151

telefon: 32 2009 462
e-mail: katarzyna.hupert-kocurek@us.edu.pl

Godziny konsultacji

poniedziałek 8.00 - 10.00

Publikacje

Felczak M.M., Sage J.M., Hupert-Kocurek K., Aykul S., Kaguni J.M. 2016. Substitutions of conserved residues in the C-terminal region of DnaC cause thermolability in helicase loading. J. Biol. Chem. doi: 10.1074/jbc.M115.708586

Hupert-Kocurek K., Wojcieszyńska D., Guzik U., Borowski T. 2015. A single amino acid substitution within catalytically non-active N-terminal domain of catechol 2,3-dioxygenase (C23O) increases enzyme activity towards 4-chlorocatechol. J. Mol. Catal. B, Enzymatic, 122, 64-71.

Domaradzka D., Guzik U., Hupert-Kocurek K., Wojcieszyńska D. 2015. Cometabolic degradation of naproxen by Planococcus sp.strain S5. Water Air Soil Pollut. 226:297, DOI 10.1007/s11270-015-2564-6.

Hupert-Kocurek K., Wojcieszyńska D., Guzik U. 2014. Activity of a carboxyl-terminal truncated form of catechol 2,3-dioxygenase from Planococcus sp. S5. Sci. World J. Article ID 598518, 9 pages.

Hupert-Kocurek K., Wojcieszyńska D., Guzik U. 2014. Altering substrate specificity of catechol 2,3-dioxygenase from Planococcus sp. strain S5 by random mutagenesis. Acta Biochimica Polonica 61, 705-710.

Hupert-Kocurek K., Banaś A., Wojcieszyńska D., Guzik U. 2014. Ukierunkowana ewolucja enzymów pochodzenia mikrobiologicznego. Post. Mikrobiol., 53, 43-48.

Guzik U., Hupert-Kocurek K., Wojcieszyńska D. 2014. Immobilization as a strategy for improving enzyme properties – application to oxidoreductases. Molecules 19, 8995-9018; doi:10.3390/ molecules19078995.

Wojcieszyńska D., Domaradzka D., Hupert-Kocurek K., Guzik U. 2014. Bacterial degradation of naproxen –undisclosed pollutant in the environment. J. Environ. Manage. 145, 157-161.

Guzik U., Hupert-Kocurek K., Sitnik M., Wojcieszyńska D. 2014. Protocatechuate 3,4-dioxygenase – a wide substrate specificity enzyme isolated from Stenotrophomonas maltophilia KB2 as a useful tool in aromatic acid biodegradation. J. Mol. Microbiol. Biotechnol. 24, 150-160.

Hupert-Kocurek K., Stawicka A., Wojcieszyńska D., Guzik U. 2013. Cloning and mutagenesis of catechol 2,3- dioxygenase gene from the gram-positive Planococcus sp. strain S5. J. Mol. Microbiol. Biotechnol. 23, 381-390.

Hupert-Kocurek K., Saczyńska A., Piotrowska-Seget Z. 2013. Cadmium increases catechol 2,3-dioxygenase activity in Variovorax sp. 12S, a metal-tolerant and phenol-degrading strain. Antonie van Leeuwenhoek, 104, 845–853.

Wojcieszyńska D., Hupert-Kocurek K., Guzik U. 2013. Influence of the entrapment of catechol 2,3-dioxygenase in κ-carrageenan on its properties. Pol. J. Environ. Stud., 22, 1219-1225