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By using pig pancreatic lipase (EC 3.1.1.3 or PPL) as a biocatalyst, covalently immobilized on amorphous AlPO 4 support, a new second generation biodiesel was obtained in the transesterification reaction of sunflower oil with ethanol. The resulting biofuel is composed of fatty acid ethyl esters and monoglycerides (FAEE/MG) blended in a 2:1 molar ratio. This novel product, which integrates glycerol as monoacylglycerols (MG) into the biofuels composition, has similar physicochemical properties as conventional biodiesel and also avoids the removal step of the by-product by washing of the biodiesel with water. Immobilization of PPL was achieved by covalent attachment of the ε-amino group of the lysine residues of PPL with the aldehyde groups of p-hydroxybenzaldehyde linked on a hybrid organic-inorganic functionalized AlPO 4 surface. With this procedure, the PPL biocatalyst was strongly fixed to the inorganic support surface (94.3%). Nevertheless, the efficiency of the immobilized enzyme was relatively lower compared to that of the free PPL, but it showed a remarkable stability as well as a great capacity of reutilization (25 reuses) without a significant loss of its initial OPEN ACCESSEnergies 2013, 6 3880 catalytic activity. Therefore, this enzymatic method allows the production of a biodiesel which integrates the glycerol, allows a more efficient fabrication method and minimizes the waste production as compared to the conventional alkali-catalyzed process.

By using 1,3-specific Pig Pancreatic lipase (EC 3.1.1.3 or PPL), covalently immobilized on AlPO4/Sepiolite support as biocatalyst, a new second-generation biodiesel was obtained in the transesterification reaction of sunflower oil with ethanol and other alcohols of low molecular weight. The resulting biofuel is composed of fatty acid ethyl esters and monoglycerides (FAEE/MG) blended in a molar relation 2/1. This novel product, which integrates glycerol as monoacylglycerols (MG) into the biofuel composition, has similar physicochemical properties compared to those of conventional biodiesel and also avoids the removal step of this by-product. The biocatalyst was found to be strongly fixed to the inorganic support (75%). Nevertheless, the efficiency of the immobilized enzyme was reduced to half (49.1%) compared to that of the free PPL. The immobilized enzyme showed a remarkable stability as well as a great reusability (more than 40 successive reuses) without a significant loss of its initial catalytic activity. Immobilized and free enzymes exhibited different reaction mechanisms, according to the different results in the Arrhenius parameters (Ln A and Ea). However, the use of supported PPL was found to be very suitable for the repetitive production of biofuel due to its facile recyclability from the reaction mixture.

Following a new methodology to obtain hybrid organic-inorganic solids, the homogeneous complex [Ru II (bpea) {(S)())(BINAP)}Cl](BF 4 ), (bpea = N,N-bis(2-pyridylmethyl)ethylamine and BINAP = 2,2¢-bis(diphenylphosphino)-1,1¢-binaphthyl) has been covalently immobilized on an AlPO 4 amorphous solid. It was tested in the successive liquid phase enantioselective hydrogenation of several prochiral substrates such us dimethyl itaconate, methyl 2-acetamidoacrylate and methyl 2-acetamidocinnamate, in CH 2 Cl 2 as solvent, ([subs]/[cat] = 0.016/0.000352 = 45.4), hydrogen pressure 6.8 atm and 50-70°C reaction temperatures. Results obtained indicate that the catalytic activity with a high enantioselectivity (99%) was maintained throughout 10 successive reactions. Furthermore, the immobilized catalyst was easily recovered when repeatedly used and handled for several days, under the same experimental conditions as those in a conventional heterogeneous supported Ru catalyst.

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