Publication: Synthesis of cetyl ricinoleate catalyzed by immobilized Lipozyme® CalB lipase in a solvent-free system.
Authors
Montiel Morte, María Claudia
; Serrano Arnaldos, Mar ; Máximo Martín, María Fuensanta ; Gómez Gómez, María ; Ortega Requena, Salvadora ; Bastida Rodriguez, Josefa
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Publisher
Elsevier
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DOI
10.1016/j.cattod.2014.09.015
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info:eu-repo/semantics/article
Description
Abstract
green 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.
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Citation
Catalysis Today (2015) 255 49–53
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