Enzymatic synthesis of perillyl alcohol derivatives and investigation of their antiproliferative activity
| dc.contributor.author | Xanthakis, E. | en |
| dc.contributor.author | Magkouta, S. | en |
| dc.contributor.author | Loutrari, H. | en |
| dc.contributor.author | Stamatis, H. | en |
| dc.contributor.author | Roussos, C. | en |
| dc.contributor.author | Kolisis, F. N. | en |
| dc.date.accessioned | 2015-11-24T16:34:19Z | |
| dc.date.available | 2015-11-24T16:34:19Z | |
| dc.identifier.issn | 1024-2422 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7791 | |
| dc.rights | Default Licence | - |
| dc.subject | perillyl alcohol | en |
| dc.subject | enzymatic glucosylation/acylation | en |
| dc.subject | glucosidase | en |
| dc.subject | lipase b | en |
| dc.subject | antitumor growth activity | en |
| dc.subject | organic media | en |
| dc.subject | candida-antarctica | en |
| dc.subject | cancer | en |
| dc.subject | solvents | en |
| dc.subject | lipase | en |
| dc.subject | chemoprevention | en |
| dc.subject | specificity | en |
| dc.subject | stability | en |
| dc.subject | acylation | en |
| dc.subject | enzymes | en |
| dc.title | Enzymatic synthesis of perillyl alcohol derivatives and investigation of their antiproliferative activity | en |
| heal.abstract | The monoterpene perillyl alcohol (POH), an intermediate in the plant terpenoid biosynthetic pathway, has well-established tumor chemopreventive and chemotherapeutic potential. We have previously shown that the primary hydroxyl group of POH is essential for its antitumor and anti-angiogenic activities. In the current study we present the enzymatic synthesis of two POH derivatives with different polar and hydrophobic characteristics, namely perillyl glucoside and perillyl glucoside fatty ester, through a two-step modification. Initial glucosylation of POH on its active hydroxyl group with D-(+)-glucose and subsequent esterification of the perillyl glucoside product with vinyl laurate were carried out using almond beta-glucosidase and lipase B from Candida antarctica, respectively, in a low-water system. Optimization of enzymatic reactions was performed to achieve the highest possible conversion yields. The antitumor cell proliferation activity against mouse Lewis lung carcinoma cells was retained in both derivatives, although the perillyl glucoside ester showed greater inhibition than perillyl glucoside. Our results underline the feasibility of enzymatically producing novel bioactive analogs of phytochemicals displaying useful physicochemical properties. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | Doi 10.1080/10242420902811089 | - |
| heal.identifier.secondary | <Go to ISI>://000268032500002 | - |
| heal.identifier.secondary | http://informahealthcare.com/doi/abs/10.1080/10242420902811089 | - |
| heal.journalName | Biocatalysis and Biotransformation | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2009 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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