Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
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:  glycine-betaine
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
EN
A reversible effect of pH on the ionization of amino-acid residues at the active center of choline oxidase was observed near the optimum pH (8). Inactivation of choline oxidase took place in the pH ranges 3-6 and 9-11, in which irreversible changes in the structure occur leading to the enzyme inactivation. The first order rate constants of the enzyme's inactivation at various pH values were estimated for the irreversible changes. The Arrhenius analysis revealed no significant changes in the activation enthalpy, while an increase in the activation entropy reflected an increase in the conformational freedom.
EN
Staphylococcus aureus is responsible for many types of infections related to biofilm presence. As the early diagnostics remains the best option for prevention of biofilm infections, the aim of the work presented was to search for differences in metabolite patterns of S. aureus ATCC6538 biofilm vs. free-swimming S. aureus planktonic forms. For this purpose, Nuclear Magnetic Resonance (NMR) spectroscopy was applied. Data obtained were supported by means of Scanning Electron Microscopy, quantitative cultures and X-ray computed microtomography. Metabolic trends accompanying S. aureus biofilm formation were found using Principal Component Analysis (PCA). Levels of isoleucine, alanine and 2,3-butanediol were significantly higher in biofilm than in planktonic forms, whereas level of osmoprotectant glycine-betaine was significantly higher in planktonic forms of S. aureus. Results obtained may find future application in clinical diagnostics of S. aureus biofilm-related infections.
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.