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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Papadopoulou, A. A. | en |
| dc.contributor.author | Katsoura, M. H. | en |
| dc.contributor.author | Chatzikonstantinou, A. | en |
| dc.contributor.author | Kyriakou, E. | en |
| dc.contributor.author | Polydera, A. C. | en |
| dc.contributor.author | Tzakos, A. G. | en |
| dc.contributor.author | Stamatis, H. | en |
| dc.date.accessioned | 2015-11-24T16:57:47Z | - |
| dc.date.available | 2015-11-24T16:57:47Z | - |
| dc.identifier.issn | 1873-2976 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10618 | - |
| dc.rights | Default Licence | - |
| dc.title | Enzymatic hybridization of alpha-lipoic acid with bioactive compounds in ionic solvents | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | 10.1016/j.biortech.2013.02.067 | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/23567667 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0960852413003027/1-s2.0-S0960852413003027-main.pdf?_tid=97d63ca6-4075-11e3-8e40-00000aab0f26&acdnat=1383036135_f3a6a96fb566dc866b8efba9d289b9ed | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2013 | - |
| heal.abstract | The lipase-catalyzed molecular hybridization of alpha-lipoic acid (LA) with bioactive compounds pyridoxine, tyrosol and tyramine was performed in ionic solvents and deep eutectic solvents. The biocatalytic reactions were catalyzed by Candida antarctica lipase B immobilized onto various functionalized multi-walled carbon nanotubes (f-CNTs-CaLB), as well as by commercial Novozym 435. The use of f-CNTs-CaLB leads, in most cases, to higher conversion yields as compared to Novozym 435. The nature and ion composition of ionic solvents affect the performance of the biocatalytic process. The highest conversion yield was observed in (mtoa)NTf2. The high enzyme stability and the relatively low solubility of substrates in specific media account for the improved biocatalytic synthesis of molecular hybrids of LA. Principal component analysis was used to screen for potential lipoxygenase inhibitors. In vitro studies showed that the synthesized compounds exhibit up to 10-fold increased inhibitory activity on lipoxygenase mediated lipid peroxidation as compared to parent molecules. | en |
| heal.publisher | Elsevier | en |
| heal.journalName | Bioresour Technol | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Papadopoulou-2013-Enzymatic hybridizat.pdf | 882.23 kB | Adobe PDF | View/Open Request a copy |
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