Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 2

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  OXIDOREDUCTASE
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1

Campylobacter protein oxidation influences epithelial cell invasion or intracellular survival as well as intestinal tract colonization in chickens

100%
Lasica A. M., Wyszynska A., Szymanek K., Majewski P., Jagusztyn-Krynicka E. K.
|
|
vol. 51
|
issue 3
383-393
EN
The Dsb family of redox proteins catalyzes disulfide bond formation and isomerization. Since mutations in dsb genes change the conformation and stability of many extracytoplasmic proteins, and since many virulence factors of pathogenic bacteria are extracytoplasmic, inactivation of dsb genes often results in pathogen attenuation. This study investigated the role of 2 membrane-bound oxidoreductases, DsbB and DsbI, in the Campylobacter jejuni oxidative Dsb pathway. Campylobacter mutants, lacking DsbB or DsbI or both, were constructed by allelic replacement and used in the human intestinal epithelial T84 cell line for the gentamicin protection assay (invasion assay) and chicken colonization experiments. In C. coli strain 23/1, the inactivation of the dsbB or dsbI gene separately did not significantly affect the colonization process. However, simultaneous disruption of both membrane-bound oxidoreductase genes significantly decreased the strain's ability to colonize chicken intestines. Moreover, C. jejuni strain 81-176 with mutated dsbB or dsbI genes showed reduced invasion/intracellular survival abilities. No cells of the double mutants (dsbB? dsbI?) of C. jejuni 81-176 were recovered from human cells after 3 h of invasion.
2

Selected issues of non-conventional enzymology. Part II ? Characterization of reaction media and biocatalysts applied in non-conventional enzymology

88%
Antczak T., Szczesna-Antczak M.
Biotechnologia
|
2003
|
issue 3
139-158
EN
Burgeoning scientific literature proves that enzymes can catalyze chemical reactions in non-conventional media, are active against liquid, solid or gaseous substrates, retain their catalytic function in organic solvents, biphasic systems composed of organic solvent and water and supercritical fluids. Non-aqueous media appeared to be a promising alternative as an environment for the reactions catalyzed by enzymes. The possibility of carrying out enzymatic processes in such unusual milieus enlarged the range of applications of biocatalysis, and solved many problems witnessed by pharmaceutical, food and chemical industries. The paper describes both advantages and disadvantages of non-conventional media, and presents the examples of practical uses of selected enzymes (lipases, proteases, oxidoreductases, glycosidases) in these systems. The details on medium composition and the form of the biocatalyst are included.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.