Publication:
Synthesis of cetyl ricinoleate catalyzed by immobilized Lipozyme® CalB lipase in a solvent-free system.

Simple item page
dc.contributor.authorMontiel Morte, María Claudia
dc.contributor.authorSerrano Arnaldos, Mar
dc.contributor.authorMáximo Martín, María Fuensanta
dc.contributor.authorGómez Gómez, María
dc.contributor.authorOrtega Requena, Salvadora
dc.contributor.authorBastida Rodriguez, Josefa
dc.contributor.departmentIngeniería Química
dc.date.accessioned2021-01-28T09:29:14Z
dc.date.available2021-01-28T09:29:14Z
dc.date.issued2015-10-15
dc.description.abstractgreen process has been performed for the synthesis of the emollient ester cetyl ricinoleate with a new immobilized derivative of Candida antarctica lipase B, which has been prepared by physical adsorption of Lipozyme® CalB L on a macroporous anionic exchange resin (Lewatit® MonoPlus MP 64). An immobilized CalB lipase with protein content over 30 mg/g has been obtained and it has been successfully used as biocatalyst to produce cetyl ricinoleate from esterification of ricinoleic acid with cetyl alcohol. Influence of amount of biocatalyst and temperature was studied in the open-air reactor, and optimal values could be fixed in 2 mg and 70ºC respectively. Biocatalyst storage stability study was developed in this reactor and it was showed the high storage stability of the immobilized derivative, because it keeps 100% of its enzymatic activity after eight months. Studies of recovery and reuse of the immobilized derivative were performed in the vacuum reactor, and it was proved the posibility of using the same biocatalyst in three consecutive reaction cycles without apparent loss of activity. Finally, the characterization of the cetyl ricinoleate obtained in the vacuum reactor demonstrated that the product obtained after only 3 or 4 hours of reaction meets manufacturers’ specifications.es
dc.formatapplication/pdfes
dc.format.extent24es
dc.identifier.citationCatalysis Today (2015) 255 49–53
dc.identifier.doi10.1016/j.cattod.2014.09.015
dc.identifier.issn0920-5861
dc.identifier.urihttp://hdl.handle.net/10201/101922
dc.languageenges
dc.publisherElsevieres
dc.relationBiosíntesis de emulsionantes con aplicaciones alimentarias y cosméticas, en sistemas "solvent-free", utilizando lipasas comerciales. MICINN CTQ2011-24091es
dc.relation.isreplacedbyhttps://www.sciencedirect.com/science/article/pii/S092058611400652Xes
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S092058611400652Xes
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.subjectCandida antarctica lipase B, Enzymatic synthesis, Solvent-free, Cetyl ricinoleate, Cosmetices
dc.subject.otherCDU::6 - Ciencias aplicadases
dc.subject.otherCDU::6 - Ciencias aplicadas::66 - Ingeniería, tecnología e industria química. Metalurgiaes
dc.titleSynthesis of cetyl ricinoleate catalyzed by immobilized Lipozyme® CalB lipase in a solvent-free system.es
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
CATTOD-2015.pdf
Size:
569.58 KB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.39 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Artículos