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Production of the recombinant thermostable beta-galactosidase [N-beta-galactosidase-his6-c and N-beta-galactosidase-thioredoxin-his6-c] from Pyrococcus woesei and immobilization study of the obtained enzymes

100%

Wanarska M. , Czartoryska I.

nr 3A

757

Beta-D-galaktozydazy - zrodla, wlasciwosci i zastosowanie

100%

Wanarska M. , Kur J.

Biotechnologia

2005

nr 4

46-62

Cloning, expression in Komagataella phaffii, and biochemical characterization of recombinant sequence variants of Pseudomonas sp. S9 GDSL-esterase

80%

Wicka-Grochowska M. , Cieslinski H. , Wanarska M.

tom 68

nr 3

Historical outline of Polish society of microbiologists, field branch in Gdansk

80%

Krawczyk B. , Komarnicka J. , Wanarska M.

Postępy Mikrobiologii. Suplement

2017

tom 56

nr 3

Thermostable Pyrococcus woesei beta-D-galactosidase - high level expression, purification and biochemical properties

80%

Wanarska M. , Kur J. , Pladzyk R. , Turkiewicz M.

2005

tom 52

nr 4

The gene encoding β-D-galactosidase from Pyrococcus woesei was PCR amplified, cloned, expressed in Escherichia coli under the control of an inducible T7 promoter, purified and characterized. The expression system was developed by the construction of recombinant plasmid, based on the high copy number pUET1 vector, giving four times more efficient expression of P. woesei β-D-galactosidase (20 mg of enzyme from 1 liter of culture) than that obtained from a previously constructed one. The recombinant enzymes were purified in a two-step procedure: double heat-denaturation of E. coli cell proteins and affinity chromatography on p-aminobenzyl 1-thio-β-D-galactopyranoside-agarose. To achieve efficient purification of P. woesei β-D-galactosidase by immobilized metal-ion affinity chromatography (IMAC), a His-tag was placed either at the N- or the C-terminal of the coding sequence. The obtained fusion proteins revealed the same specific activity of approximately 5400 U/mg, which was 10 times lower than the wild-type β-D-galactosidase (51100 U/mg). The activity of P. woesei β-D-galactosidase was enhanced by thiol compounds, Mg2+ ions and D-galactose, and was inhibited by heavy metal ions and D-glucose, while Ca2+ ions had no effect.

A freeze-thaw method for disintegration of Escherichia coli cells producing T7 lysozyme used in pBAD expression systems

80%

Wanarska M. , Hildebrandt P. , Kur J.

tom 54

nr 3

The pLysN plasmid containing the T7 lysozyme gene under control of the lac promoter was constructed to facilitate cell disintegration after expression of recombinant proteins in arabinose-induced expression systems. The usefulness of this plasmid was tested in Escherichia coli TOP10 and E. coli LMG194 cells carrying pBADMHADgeSSB plasmid containing Deinococcus geothermalis SSB protein gene under control of the araBAD promoter. The results showed that low-level expression of T7 lysozyme did not interfere with the target SSB protein production, and that the freezing-thawing treatment was sufficient for disruption of the E. coli cells producing low amounts of T7 lysozyme.

Wykorzystanie glicerolu jako źródła węgla do produkcji adaptowanych do zimna beta-galaktozydaz przez rekombinantowe szczepy drożdży Pichia pastoris

70%

Wanarska M. , Baranski J. , Krajewska E. , Wicka-Grochocka M. , Cieslinski H.

nr 2

Biosynteza esterazy z Pseudomonas sp. S9 w komórkach Pichia pastoris, oczyszczanie i charakterystyka

61%

Wicka-Grodzka M. , Terebieniec A. , Krajewska E. , Filipowicz N. , Cieslinski H. , Wanarska M.

nr 2

Cloning, expression, and biochemical characterization of a coldactive GDSL-esterase of a Pseudomonas sp. S9 isolated from Spitsbergen island soil

61%

Wicka M. , Wanarska M. , Krajewska E. , Pawlak-Szukalska A. , Kur J. , Cieslinski H.

Acta Biochimica Polonica

2016

tom 63

nr 1