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Journal ArticleDOI

Overcoming the Incompatibility Challenge in Chemoenzymatic and Multi-Catalytic Cascade Reactions.

TLDR
This Minireview will summarize recent synthetic examples of (chemo)enzymatic cascade reactions and outline promising methods for their spatial control either by using bio-derived or synthetic systems.
Abstract
Multi-catalytic cascade reactions bear a great potential to minimize downstream and purification steps, leading to a drastic reduction of the produced waste. In many examples, the compatibility of chemo- and biocatalytic steps could be easily achieved. Problems associated with the incompatibility of the catalysts and their reactions, however, are very frequent. Cascade-like reactions can hardly occur in this way. One possible solution to combine, in principle, incompatible chemo- and biocatalytic reactions is the defined control of the microenvironment by compartmentalization or scaffolding. Current methods for the control of the microenvironment of biocatalysts go far beyond classical enzyme immobilization and are thus believed to be very promising tools to overcome incompatibility issues and to facilitate the synthetic application of cascade reactions. In this Minireview, we will summarize recent synthetic examples of (chemo)enzymatic cascade reactions and outline promising methods for their spatial control either by using bio-derived or synthetic systems.

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Journal ArticleDOI

Opportunities and challenges for combining chemo- and biocatalysis

TL;DR: This Review focuses on efforts to combine chemo- and biocatalysts, outlining the opportunities achievable by this approach and also efforts to overcome any incompatibilities between these different systems.
Journal ArticleDOI

Biocatalytic Oxidation Reactions: A Chemist's Perspective

TL;DR: The most important recent developments in the field of biocatalytic oxidation chemistry are critically summarised and the most pressing bottlenecks as well as promising solutions are identified.
Journal ArticleDOI

Photo-Biocatalysis: Biotransformations in the Presence of Light

TL;DR: An overview of the various approaches for using light in biocatalysis is given and enzymes with a light switchable moiety have been investigated to turn off/on or tune the actual reaction.
Journal ArticleDOI

On the taught new tricks of enzymes immobilization: An all-inclusive overview

TL;DR: This review describes the choices of support materials and cross-linkers together with several mechanisms that influence the performance, stabilization and hyperactivation of immobilized enzymes.
References
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Journal ArticleDOI

Integrated catalysis opens new arylation pathways via regiodivergent enzymatic C-H activation

TL;DR: Integration of regioselective halogenase enzymes with Pd-catalysed cross-coupling chemistry, in one-pot reactions, successfully addresses the problem of discrimination between two similar, unactivated C–H positions for the indole heterocycle, and delivers a range of functionally diverse arylated products.
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Cross-linked polymersomes as nanoreactors for controlled and stabilized single and cascade enzymatic reactions

TL;DR: Cross-linked and pH sensitive polymersomes provide a basis for pH controlled enzymatic reactions where no integrated transmembrane protein is needed for regulating the uptake and release of educts and products in the polymersome lumen.
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Viruses and protein cages as nanocontainers and nanoreactors

TL;DR: In this paper, the use of viral capsids and other protein cages as nanocontainers and nanoreactors is discussed, and the templating of chemical reactions within these biological hollow scaffolds has allowed the synthesis of inorganic materials with nanoscale dimensions.
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Design of Surface-Active Artificial Enzyme Particles to Stabilize Pickering Emulsions for High-Performance Biphasic Biocatalysis.

TL;DR: Surface-active artificial enzymes can simultaneously stabilize Pickering emulsions and catalyze biphasic biotransformation with superior enzymatic stability and good re-usability and are useful for interfacial conversion of hydrophobic p-nitrophenyl butyrate into yellow water-soluble p-Nitrophenolate catalyzed by esterase-mimic SAE.
Journal ArticleDOI

Efficient in vitro encapsulation of protein cargo by an engineered protein container.

TL;DR: An engineered variant of lumazine synthase, a nonviral capsid protein with a negatively charged luminal surface, is shown to encapsulate up to 100 positively supercharged green fluorescent protein (GFP) molecules in vitro, providing excellent control over packing density.
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