Biocatalysis using microemulsion-based polymer gels containing lipase
dc.contributor.author | Stamatis, Haralambos | en |
dc.contributor.author | Xenakis, Aristotelis | en |
dc.date.accessioned | 2015-11-24T16:32:16Z | |
dc.date.available | 2015-11-24T16:32:16Z | |
dc.identifier.issn | 1381-1177 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7535 | |
dc.rights | Default Licence | - |
dc.subject | Biocatalysis | en |
dc.subject | Microemulsion | en |
dc.subject | Polymer gel | en |
dc.subject | Lipase | en |
dc.subject | Esterification | en |
dc.title | Biocatalysis using microemulsion-based polymer gels containing lipase | en |
heal.abstract | Natural gelling agents such as gelatin, agar and ΞΊ-carrageenan have been tested for the formation of lecithin microemulsion-based gels as well as hydrogels (without surfactant and oil). The results presented in this work provide information concerning the utility of these solid gels as lipase immobilization matrices. It was found that lipase from Pseudomonas cepacia keeps its catalytic function after entrapment in the gels, catalyzing the esterification reaction of propanol with lauric acid in various hydrocarbons at room temperature. Various parameters which affect the lipase catalytic behavior such as the nature and the concentration of the gelling agent, as well as the concentration of the biocatalyst and the mole ratio of the substrates have been examined. High yields (80%) were obtained with agar and ΞΊ-carrageenan organogels in isooctane. The remaining lipase activity, in repeated syntheses was found to depend on the nature of the biopolymer used for the formation of the organogels. Gelatin and agar microemulsion-based gels showed the highest operational stability. | en |
heal.access | campus | - |
heal.fullTextAvailability | TRUE | - |
heal.identifier.primary | 10.1016/s1381-1177(98)00142-8 | - |
heal.identifier.secondary | http://www.sciencedirect.com/science/article/pii/S1381117798001428 | - |
heal.journalName | Journal of Molecular Catalysis B: Enzymatic | en |
heal.journalType | peer reviewed | - |
heal.language | en | - |
heal.publicationDate | 1999 | - |
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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