Enzyme-based Biohybrid Foams Designed for Biodiesel Production and Continuous Flow Heterogeneous Catalysis
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Enzyme-based Biohybrid Foams Designed for Biodiesel Production and Continuous Flow Heterogeneous Catalysis Nicolas Brun,1 Hervé Deleuze2 and Rénal Backov1 1
Centre de Recherche Paul Pascal, UPR 8641-CNRS, Université de Bordeaux, 115 Avenue
Albert Schweitzer, 33600 Pessac, France. 2
Université de Bordeaux, Institut des Sciences Moléculaires (ISM) UMR-5255-CNRS, 351
Cours de la Libération, 33405 Talence, France.
ABSTRACT The one pot-synthesis and use of monolithic biohybrid foams in a continuous flow device reported inhere presents the advantages of covalent stabilization of the enzymes, together with a low steric hindrance between proteins and substrates, an optimized mass transport due to the interconnected macroporous network and a rather simplicity in regard of the column in-situ synthetic path. Those features, concerning transesterification (biodiesel production) enzymebased catalyzed reaction, provide high enzymatic activity addressed with bio-hybrid catalysts bearing unprecedented endurance of continuous catalysis for a two months period of time. INTRODUCTION Modern societies will be confronted in the near future to an increasing requirement of fuels combined with a programmed diminution of easily extractable resources of fossil origin. In this context, biodiesels, which are fatty acid methyl or ethyl esters obtained by transesterification of vegetable oils has attracted considerable attention during the last decade[1]. Several processes for biodiesel fuel production have been developed, among which transesterification with alcohol using mineral acids[2], or bases[3] catalysts are the most common. Alkali-catalyzed alcoholysis, which is about 4000 times faster than its acid catalyzed counterpart, is commonly used in industrial processes[3]. Recently, enzymatic transesterification using lipases (triacylglycerol hydrolases), has become an interesting alternative for biodiesel fuel production, since the problems mentioned above can be circumvented[4]. In such context, it is necessary to develop processes insuring a complete recyclability and stability of enzymatic catalysts over the time, in order to reduce the impact of this cost increase down to competitive levels. Immobilization or entrapment of biocatalysts[5], onto or within porous materials using either physical adsorption,[6] covalent attachment[7], inclusion or encapsulation by sol-gel route,[8] represent an attractive and efficient approach to facilitate their use in continuous devices, and to compete with cheaper processes [9-13]. Therefore, the design of new functional porous materials to immobilize active biomacromolecules still present a challenge of both economic and ecological interests.
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EXPERIMENTAL DETAILS Syntheses. Tetraethylorthosilane (TEOS), tetradecyltrimethylammonium bromide (TTAB), (3-Glycidyloxypropyl)trimethoxysilane and dodecane were purchased from Fluka (St. Louis, MO). Lipase from Thermomyces Lanuginosus (solution, ≥100,000 U/g), carthame oil (Purified Safflower Oil), oleic acid, glyceryl trilinoleate (98 %), ethyl linoleat
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