Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine
Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (ac...
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| Format: | Article |
| Language: | English |
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MDPI AG
2012-11-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/17/12/13813 |
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| author | Marcela Krečmerová Marie Zarevúcka Lucie Janská Jiří Blažek Jana Brabcová |
| author_facet | Marcela Krečmerová Marie Zarevúcka Lucie Janská Jiří Blažek Jana Brabcová |
| author_sort | Marcela Krečmerová |
| collection | DOAJ |
| description | Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (acetate, butyrate, decanoate, laurate, palmitate). The transesterification activities of these immobilized enzymes were compared with commercially available lipases (lipase from hog pancreas, Aspergillus niger, Candida antarctica, Pseudomonas fluorescens). Lipase from Candida antarctica was found to be the most efficient enzyme regarding chemical yield of the desired products, while transesterification by lipase from Aspergillus niger resulted in lower yields. |
| first_indexed | 2024-12-11T08:05:17Z |
| format | Article |
| id | doaj.art-6b66f8245be3487daf1cf04b03381ad7 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-11T08:05:17Z |
| publishDate | 2012-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-6b66f8245be3487daf1cf04b03381ad72022-12-22T01:15:01ZengMDPI AGMolecules1420-30492012-11-011712138131382410.3390/molecules171213813Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenineMarcela KrečmerováMarie ZarevúckaLucie JanskáJiří BlažekJana BrabcováLipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (acetate, butyrate, decanoate, laurate, palmitate). The transesterification activities of these immobilized enzymes were compared with commercially available lipases (lipase from hog pancreas, Aspergillus niger, Candida antarctica, Pseudomonas fluorescens). Lipase from Candida antarctica was found to be the most efficient enzyme regarding chemical yield of the desired products, while transesterification by lipase from Aspergillus niger resulted in lower yields.http://www.mdpi.com/1420-3049/17/12/13813lipasetransesterificationprodrugimmobilization of enzymes |
| spellingShingle | Marcela Krečmerová Marie Zarevúcka Lucie Janská Jiří Blažek Jana Brabcová Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine Molecules lipase transesterification prodrug immobilization of enzymes |
| title | Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine |
| title_full | Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine |
| title_fullStr | Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine |
| title_full_unstemmed | Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine |
| title_short | Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine |
| title_sort | lipases as tools in the synthesis of prodrugs from racemic 9 2 3 dihydroxypropyl adenine |
| topic | lipase transesterification prodrug immobilization of enzymes |
| url | http://www.mdpi.com/1420-3049/17/12/13813 |
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