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Biocatalytic Behaviour of Immobilized Rhizopus oryzae Lipase in the 1,3-Selective Ethanolysis of Sunflower Oil to Obtain a Biofuel Similar to Biodiesel

1
Department of Organic Chemistry, University of Cordoba, Campus de Rabanales, Ed. Marie Curie, Córdoba 14014, Spain
2
Crystallographic Studies Laboratory, Andalusian Institute of Earth Sciences, CSIC, Avda. Las Palmeras 4, Armilla 18100, Granada, Spain
3
Department of Microbiology, University of Córdoba, Campus de Rabanales, Ed. Severo Ochoa, Córdoba 14014, Spain
4
Seneca Green Catalyst S.L., Campus de Rabanales, Córdoba 14014, Spain
*
Author to whom correspondence should be addressed.
Molecules 2014, 19(8), 11419-11439; https://doi.org/10.3390/molecules190811419
Received: 5 May 2014 / Revised: 22 July 2014 / Accepted: 22 July 2014 / Published: 4 August 2014
(This article belongs to the Special Issue Enzyme Immobilization)
A new biofuel similar to biodiesel was obtained in the 1,3-selective transesterification reaction of sunflower oil with ethanol using as biocatalyst a Rhizopus oryzae lipase (ROL) immobilized on Sepiolite, an inorganic support. The studied lipase was a low cost powdered enzyme preparation, Biolipase-R, from Biocon-Spain, a multipurpose additive used in food industry. In this respect, it is developed a study to optimize the immobilization procedure of these lipases on Sepiolite. Covalent immobilization was achieved by the development of an inorganic-organic hybrid linker formed by a functionalized hydrocarbon chain with a pendant benzaldehyde, bonded to the AlPO4 support surface. Thus, the covalent immobilization of lipases on amorphous AlPO4/sepiolite (20/80 wt %) support was evaluated by using two different linkers (p-hydroxybenzaldehyde and benzylamine-terephthalic aldehyde, respectively). Besides, the catalytic behavior of lipases after physical adsorption on the demineralized sepiolite was also evaluated. Obtained results indicated that covalent immobilization with the p-hydroxybenzaldehyde linker gave the best biocatalytic behavior. Thus, this covalently immobilized lipase showed a remarkable stability as well as an excellent capacity of reutilization (more than five successive reuses) without a significant loss of its initial catalytic activity. This could allow a more efficient fabrication of biodiesel minimizing the glycerol waste production. View Full-Text
Keywords: biodiesel; immobilization; Rhizopus oryzae lipase; Biolipase-R; amorphous AlPO4/sepiolite; demineralized sepiolite; selective transesterification; monoglyceride; Ecodiesel; sunflower oil biodiesel; immobilization; Rhizopus oryzae lipase; Biolipase-R; amorphous AlPO4/sepiolite; demineralized sepiolite; selective transesterification; monoglyceride; Ecodiesel; sunflower oil
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Luna, C.; Verdugo, C.; Sancho, E.D.; Luna, D.; Calero, J.; Posadillo, A.; Bautista, F.M.; Romero, A.A. Biocatalytic Behaviour of Immobilized Rhizopus oryzae Lipase in the 1,3-Selective Ethanolysis of Sunflower Oil to Obtain a Biofuel Similar to Biodiesel. Molecules 2014, 19, 11419-11439.

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