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https://olympias.lib.uoi.gr/jspui/handle/123456789/7660Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Skouridou, V. | en |
| dc.contributor.author | Chrysina, E. D. | en |
| dc.contributor.author | Stamatis, H. | en |
| dc.contributor.author | Oikonomakos, N. G. | en |
| dc.contributor.author | Kolisis, F. N. | en |
| dc.date.accessioned | 2015-11-24T16:33:26Z | - |
| dc.date.available | 2015-11-24T16:33:26Z | - |
| dc.identifier.issn | 1381-1177 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7660 | - |
| dc.rights | Default Licence | - |
| dc.subject | biocatalysis | en |
| dc.subject | lipase | en |
| dc.subject | enantioselectivity | en |
| dc.subject | molecular modelling | en |
| dc.subject | monoterpene perillyl alcohol | en |
| dc.subject | protein structures | en |
| dc.subject | structural basis | en |
| dc.subject | cepacia lipase | en |
| dc.title | Kinetic and modelling studies on the lipase catalysed enantio selective esterification of (+/-)-perillyl alcohol | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | DOI 10.1016/j.molcatb.2004.02.011 | - |
| heal.identifier.secondary | <Go to ISI>://000221882900003 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S1381117704000529/1-s2.0-S1381117704000529-main.pdf?_tid=54489d15d19a8cfbdb25f5c4556f1375&acdnat=1335510586_52f9a5a3660026d82534fb59bc9af8e8 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 2004 | - |
| heal.abstract | Several lipases were kinetically studied with the aim to exploit their enantioselectivity in the esterification of (S)-(-) and (R)-(+)-perillyl alcohol with decanoic acid. Most of the lipases studied exhibited stereopreference towards the R-enantiomer with apparent E-values from 3.8 to 0.6, calculated as the initial esterification rates ratio for the individual enantiomers. In an attempt to interpret the structural basis of enantioselectivity, modelling studies were performed with two of these lipases, Candida cylindracea lipase (CcL) and Pseudomonas cepacia lipase (PcL) based on their previously determined X-ray crystal structures. The results derived from modelling studies confirm their stereopreferences towards the R-enantiomer, since increased conformational energy of the S-ester was found compared to the R-ester. (C) 2004 Elsevier B.V. All rights reserved. | en |
| heal.journalName | Journal of Molecular Catalysis B-Enzymatic | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Skouridou-2004-Kinetic and modellin.pdf | 112.78 kB | Adobe PDF | View/Open Request a copy |
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