Structural and functional catalytic characteristics of cross-linked enzyme aggregates (CLEA) are reviewed. Firstly, advantages of enzyme immobilization and existing types of immobilization are described. Then, a wide description of the factors that modify CLEA activity, selectivity and stability is presented. Nowadays CLEA offers an economic, simple and easy tool to reuse biocatalysts, improving their catalytic properties and stability. This immobilization methodology has been widely and satisfactorily tested with a great variety of enzymes and has demonstrated its potential as a future tool to optimize biocatalytic processes.
Microfluidic reaction devices are a very promising technology for chemical and biochemical processes. In microreactors, the micro dimensions, coupled with a high surface area/volume ratio, permit rapid heat exchange and mass transfer, resulting in higher reaction yields and reaction rates than in conventional reactors. Moreover, the lower energy consumption and easier separation of products permit these systems to have a lower environmental impact compared to macroscale, conventional reactors. Due to these benefits, the use of microreactors is increasing in the biocatalysis field, both by using enzymes in solution and their immobilized counterparts. Following an introduction to the most common applications of microreactors in chemical processes, a broad overview will be given of the latest applications in biocatalytic processes performed in microreactors with free or immobilized enzymes. In particular, attention is given to the nature of the materials used as a support for the enzymes and the strategies employed for their immobilization. Mathematical and engineering aspects concerning fluid dynamics in microreactors were also taken into account as fundamental factors for the optimization of these systems.
A general dependence of the enzyme catalytic rate on its mass was revealed when a statistical analysis of 17065 records from the EMP database was performed. The estimated activation energy of the catalytic process decreases asymptotically with the enzyme molecular mass increase. The proposed theoretical model postulates the existence of an intermediate complex of the enzyme and the departing product. It allows for the explanation of the discovered mass-energy relationship, as an effect of the global enzyme-product interactions during complex dissociation. Fitted parameters of the model seem to be in agreement with those widely accepted for the van der Waals energy of molecular interactions. Their values also agree with the picture of the hydrogen bonding in the catalytic process and suggest that surface walk can be the favorable way of the product departure.
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.