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

help Sort By:

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

Hydantoinases ? significance and applications in biotechnology

100%
Latacz G., Pekala E., Kiec-Kononowicz K.
Biotechnologia
|
2006
|
issue 2
189-205
EN
Hydantoinase is an industrial enzyme widely used for the synthesis of nonnatural D- or L-amino acids. Optically pure amino acids are required for production of semisynthetic antibiotics, active peptides or agrochemicals such as pesticides, herbicides, pyrethroides, and are important as feed and food additives. Major advantages of application of hydantoinase in industry are: high efficiency, stereoselectivity, easy production of substrates for enzyme and environment friendly alternative to chemical methods.
2

Enantioselective bioreduction of propentofylline using yeast in water and organic solvents

100%
Pekala E., Latacz G., WojciK T.
Biotechnologia
|
2007
|
issue 2
174-180
EN
Propentofylline (PPT) is a drug used in the treatment of both vascular dementia and Alzheimer type dementia. Hydroxy-metabolites of propentofylline (OHPPT) also demonstrate the same biological activity as the parent compound. As steroisomers of HOPPT are not commercially available, we had to produce them for pharmacological and pharmacokinetic studies. The aim of this study was to find the strains of Saccharomyces cerevisiae yielding enantiomerically pure (R)- or (S)-1-(5-hydroxyhexyl)-3,5-dimethyl-7-propylxanthin (OHPPT) from PPT. In this paper, we present the results of stereoselective reduction of PPT into OHPPT when catalysed by whole cells of baker's and a few strains of wine yeast in water and organic solvents.
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.