Cascade Reactions with Incompatible Catalysts and Nanoencapsulation

Cascade Reactions with Incompatible Catalysts and Nanoencapsulation 

The three different enzymes used in combination in this system were FateDH, FaldDH, andADH. FateDH catalyzes the initial reduction of C02 to formate, FaldDH the reduction of formate to formaldehyde, and ADH the reduction of formaldehyde to methanol. Interestingly, the enzymes when immobilized were more active than a combination of the free enzymes, which is claimed to be due to a reduction of spatial interference among the different enzymes. Moreover, due to the immobilization of enzymes within the microreactor, the intermediate species have significantly reduced distances to travel between active sites [21, 22]. 

The encapsulation process used was the LbL method, employing alternately charged polymers, namely PDA [poly(diallyldimethylammonium chloride)] and PSS 

DKR with lipase TL (from Pseudomonas stutzeri) was part of the reaction scheme in work reported by Hoyos et al. [24]. Here the lipase is immobilized using a number of 

Unlike in the previous example, here the catalysts are not reported specifically to deactivate one another. Rather, the immobilization of the lipase in these silica elastomer spheres allows access to reaction conditions that are otherwise unavailable, namely higher temperatures, as the lipase is no longer deactivated and is able to undergo multiple reaction cycles, resulting in a much higher enzyme productivity, in terms of mass of product per unit mass of protein. The activity of the lipase is also observed to have increased, possibly not only from its ability to access higher temperatures when immobilized, but also due to the increased stability of the active 

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