A Review on Bio-Based Catalysts (Immobilized Enzymes) Used for Biodiesel Production

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Abstract

The continuous increase of the world’s population results in an increased demand for energy drastically from the industrial and domestic sectors as well. Moreover, the current public awareness regarding issues such as pollution and overuse of petroleum fuel has resulted in the development of research approaches concerning alternative renewable energy sources. Amongst the various options for renewable energies used in transportation systems, biodiesel is considered the most suitable replacement for fossil-based diesel. In what concerns the industrial application for biodiesel production, homogeneous catalysts such as sodium hydroxide, potassium hydroxide, sulfuric acid, and hydrochloric acid are usually selected, but their removal after reaction could prove to be rather complex and sometimes polluting, resulting in increases on the production costs. Therefore, there is an open field for research on new catalysts regarding biodiesel production, which can comprise heterogeneous catalysts. Apart from that, there are other alternatives to these chemical catalysts. Enzymatic catalysts have also been used in biodiesel production by employing lipases as biocatalysts. For economic reasons, and reusability and recycling, the lipases urged to be immobilized on suitable supports, thus the concept of heterogeneous biocatalysis comes in existence. Just like other heterogeneous catalytic materials, this one also presents similar issues with inefficiency and mass-transfer limitations. A solution to overcome the said limitations can be to consider the use of nanostructures to support enzyme immobilization, thus obtaining new heterogeneous biocatalysts. This review mainly focuses on the application of enzymatic catalysts as well as nano(bio)catalysts in transesterification reaction and their multiple methods of synthesis.

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Magnetic nanoparticles: synthesis, protection, functionalization, and application.

An-Hui Lu, E L Salabas, Ferdi Schüth (2007)

This review focuses on the synthesis, protection, functionalization, and application of magnetic nanoparticles, as well as the magnetic properties of nanostructured systems. Substantial progress in the size and shape control of magnetic nanoparticles has been made by developing methods such as co-precipitation, thermal decomposition and/or reduction, micelle synthesis, and hydrothermal synthesis. A major challenge still is protection against corrosion, and therefore suitable protection strategies will be emphasized, for example, surfactant/polymer coating, silica coating and carbon coating of magnetic nanoparticles or embedding them in a matrix/support. Properly protected magnetic nanoparticles can be used as building blocks for the fabrication of various functional systems, and their application in catalysis and biotechnology will be briefly reviewed. Finally, some future trends and perspectives in these research areas will be outlined.

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Modifying enzyme activity and selectivity by immobilization.

Rafael C Rodrigues, Claudia Ortiz, Angel Berenguer-Murcia … (2013)

Immobilization of enzymes may produce alterations in their observed activity, specificity or selectivity. Although in many cases an impoverishment of the enzyme properties is observed upon immobilization (caused by the distortion of the enzyme due to the interaction with the support) in some instances such properties may be enhanced by this immobilization. These alterations in enzyme properties are sometimes associated with changes in the enzyme structure. Occasionally, these variations will be positive. For example, they may be related to the stabilization of a hyperactivated form of the enzyme, like in the case of lipases immobilized on hydrophobic supports via interfacial activation. In some other instances, these improvements will be just a consequence of random modifications in the enzyme properties that in some reactions will be positive while in others may be negative. For this reason, the preparation of a library of biocatalysts as broad as possible may be a key turning point to find an immobilized biocatalyst with improved properties when compared to the free enzyme. Immobilized enzymes will be dispersed on the support surface and aggregation will no longer be possible, while the free enzyme may suffer aggregation, which greatly decreases enzyme activity. Moreover, enzyme rigidification may lead to preservation of the enzyme properties under drastic conditions in which the enzyme tends to become distorted thus decreasing its activity. Furthermore, immobilization of enzymes on a support, mainly on a porous support, may in many cases also have a positive impact on the observed enzyme behavior, not really related to structural changes. For example, the promotion of diffusional problems (e.g., pH gradients, substrate or product gradients), partition (towards or away from the enzyme environment, for substrate or products), or the blocking of some areas (e.g., reducing inhibitions) may greatly improve enzyme performance. Thus, in this tutorial review, we will try to list and explain some of the main reasons that may produce an improvement in enzyme activity, specificity or selectivity, either real or apparent, due to immobilization.