Over the centuries mankind has always profited from biocatalytic processes in the production of wine, beer, and bread for example. Despite the technological knowledge available for thousands of years in these fermentation processes, interestingly only in the last two hundred years scientists have developed the concepts and tools that allow chemists and biochemists to use the natural power of biocatalysts in a non-natural way in the laboratory.  Despite all these achievements, some drawbacks still persists in the context of its use in the organic chemistry laboratory. In the case where isolated enzymes are used, these drawbacks are related to the stability, purity of the enzyme, availability and the necessity of co-factors. Due to the reasons cited above is not surprisingly that the use of isolated lipases has become by far the most developed transformations in biocatlyzed organic reactions, most of the success is related to their stability in organic solvent, high availability, low cost, the non-necessity of co-factors and promiscuity.  For industrial purposes the use of free lipases in batch reactors can be in some cases the most advantageous way of working due to the high cost of the immobilized enzyme and consequent need of recyclability for the biocatalyst. Another issue that should be addressed when working with immobilized enzyme is the support resistance for mechanical stress. When working with this kind of support, mechanical stirring batch reactors can damage the surface of the support leading to protein lixiviation and consequent loss of recyclability.  In this work we have optimized several biocatalytic continuous flow processes with packed bed reactors such as; esterification between solketal and stearic acid, partial hydrolysis of Palm Oil to the production of diacylglycerols and kinetic resolution of amines and alcohols.

Towards the use of lipases under continuous flow conditions

245th National Meeting (2013)

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