Towards efficient chemical synthesis via engineering enzyme catalysis in biomimetic nanoreactors

Abstract

Biocatalysis with immobilized enzymes as catalysts holds enormous promise in developing more efficient and sustainable processes for the synthesis of fine chemicals, chiral pharmaceuticals and biomass feedstocks. Despite the appealing potentials, nowadays the industrial-scale application of biocatalysts is still quite modest in comparison with that of traditional chemical catalysts. A critical issue is that the catalytic performance of enzymes, the sophisticated and vulnerable catalytic machineries, strongly depends on their intracellular working environment; however the working circumstances provided by the support matrix are radically different from those in cells. This often leads to various adverse consequences on enzyme conformation and dynamic properties, consequently decreasing the overall performance of immobilized enzymes with regard to their activity, selectivity and stability. Engineering enzyme catalysis in support nanopores by mimicking the physiological milieu of enzymes in vivo and investigating how the interior microenvironment of nanopores imposes an influence on enzyme behaviors in vitro are of paramount significance to modify and improve the catalytic functions of immobilized enzymes. In this feature article, we have summarized the recent advances in mimicking the working environment and working patterns of intracellular enzymes in nanopores of mesoporous silica-based supports. Especially, we have demonstrated that incorporation of polymers into silica nanopores could be a valuable approach to create the biomimetic microenvironment for enzymes in the immobilized state.

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

“…Structure of open form of BCL. The catalytic triad in the active site is shown in a red stick representation (Liu, Yang, & Li, )…”

The new breed of cutting-edge catalysts

“…Li, for example, is experimenting with housing enzymes inside nanoparticles 14 to help them last longer. Others are synthesizing completely artificial enzymes 15 using techniques from synthetic biology.…”

Cell Membrane-Based Nanoreactor To Mimic the Bio-Compartmentalization Strategy of a Cell

“… 47 − 49 This decrease of catalytic reaction and the resulting slow reaction that occurred particularly in porous silica nanoparticles, as previously reported, 13 depended on different factors such as modification of the enzyme structure, adsorption of the enzyme on the porous materials crowding effects and diffusion of molecules through the membranes. 50 , 51 Furthermore, the decrease of V max values for H 2 O 2 depended on the disruption of the enzyme that was affected by the confinement of HRP inside the nanoreactor compartment, 13 or due to the diffusional resistance of substrates. 52 − 54 In such a way, we previously demonstrated that UnPSi nanoparticles coated with cancer cell membranes favored the interaction between AR with the hydrophobic counterpart of bilayer membrane and hindered the enzymatic interaction with HRP, 13 thus causing slow values of V max of nanoparticles compared to the free HPR in solution.…”