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Catalysts
Special Issues
Biocatalytic Cascade Reactions (in vivo and in vitro)
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Biocatalytic Cascade Reactions (in vivo and in vitro)

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (31 July 2021) | Viewed by 10098

Special Issue Editors

Dr. Sandy Schmidt

E-Mail Website
Guest Editor
Groningen Research Institute of Pharmacy, Chemical and Pharmaceutical Biology, Anthonius Deusinglaan 1, 9713AV Groningen, The Netherlands
Interests: Main research interests focus on the design and assembly of synthetic metabolic pathways and multi-enzymatic cascades as well as the application of enzyme engineering and computational design for the development of new biocatalytic and regulatory functions. Of further interest is the investigation of electron transfer pathways in oxidoreductases and light-driven biocatalytic processes as well as structure–function relationships of dioxygenases and ferredoxin-dependent enzymes and their interactions.
Dr. Thomas Bayer

E-Mail Website
Guest Editor
Institute of Biochemistry, University of Greifswald, 17489 Greifswald, Germany
Interests: biocatalysis; whole-cell biotransformation; biosynthesis; biosensor
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The discovery of novel enzymes and their customization by protein engineering techniques is rapidly expanding the toolbox of biocatalysts available for the synthesis of value-added chemicals—both natural and non-natural compounds. Enzymes with their inherently high chemo-, regio-, and stereo-specificities can efficiently operate in vitro and in vivo. In the last two decades, the combination of multiple biocatalysts in (artificial) cascades has yielded awe-inspiring complex molecules from rather simple precursors, while the design and optimization of such cascade reactions has addressed social and environmental concerns including the stewardship of resources and the reduction of waste.

The topic of this Special Issue encompasses cascades employing (engineered) enzymes that operate simultaneously in one pot—either a reaction tube or a living cell—or in a sequential fashion in vitro, in vivo, or in hybrid systems. Enzymes may be applied in isolated form, immobilized, as cell-free extracts, as whole-cell biocatalysts, as well as in combination with metal- and organo-catalysts or in entirely unprecedented forms.

The aim of this Special Issue is to highlight current developments in the fields of biocatalysis and cascade design and to grasp emerging trends that will facilitate the manufacturing of chemicals, pharmaceuticals, and highly demanded ingredients of the future … already today!

Dr. Sandy Schmidt
Dr. Thomas Bayer
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • biocatalysis 
  • (artificial) enzyme cascades 
  • biotransformations 
  • whole-cell catalysis 
  • metabolic pathways 
  • cofactors 
  • chemo-enzymatic synthesis 
  • microbial cell factories 
  • synthetic biology

Published Papers (3 papers)

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Research

18 pages, 2703 KiB  
Article
Two (Chemo)-Enzymatic Cascades for the Production of Opposite Enantiomers of Chiral Azidoalcohols
by Elia Calderini, Philipp Süss, Frank Hollmann, Rainer Wardenga and Anett Schallmey
Catalysts 2021, 11(8), 982; https://doi.org/10.3390/catal11080982 - 17 Aug 2021
Cited by 4 | Viewed by 2355
Abstract
Multi-step cascade reactions have gained increasing attention in the biocatalysis field in recent years. In particular, multi-enzymatic cascades can achieve high molecular complexity without workup of reaction intermediates thanks to the enzymes’ intrinsic selectivity; and where enzymes fall short, organo- or metal catalysts [...] Read more.
Multi-step cascade reactions have gained increasing attention in the biocatalysis field in recent years. In particular, multi-enzymatic cascades can achieve high molecular complexity without workup of reaction intermediates thanks to the enzymes’ intrinsic selectivity; and where enzymes fall short, organo- or metal catalysts can further expand the range of possible synthetic routes. Here, we present two enantiocomplementary (chemo)-enzymatic cascades composed of either a styrene monooxygenase (StyAB) or the Shi epoxidation catalyst for enantioselective alkene epoxidation in the first step, coupled with a halohydrin dehalogenase (HHDH)-catalysed regioselective epoxide ring opening in the second step for the synthesis of chiral aliphatic non-terminal azidoalcohols. Through the controlled formation of two new stereocenters, corresponding azidoalcohol products could be obtained with high regioselectivity and excellent enantioselectivity (99% ee) in the StyAB-HHDH cascade, while product enantiomeric excesses in the Shi-HHDH cascade ranged between 56 and 61%. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions (in vivo and in vitro))
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17 pages, 3102 KiB  
Article
LuxAB-Based Microbial Cell Factories for the Sensing, Manufacturing and Transformation of Industrial Aldehydes
by Thomas Bayer, Aileen Becker, Henrik Terholsen, In Jung Kim, Ina Menyes, Saskia Buchwald, Kathleen Balke, Suvi Santala, Steven C. Almo and Uwe T. Bornscheuer
Catalysts 2021, 11(8), 953; https://doi.org/10.3390/catal11080953 - 10 Aug 2021
Cited by 8 | Viewed by 4126
Abstract
The application of genetically encoded biosensors enables the detection of small molecules in living cells and has facilitated the characterization of enzymes, their directed evolution and the engineering of (natural) metabolic pathways. In this work, the LuxAB biosensor system from Photorhabdus luminescens was [...] Read more.
The application of genetically encoded biosensors enables the detection of small molecules in living cells and has facilitated the characterization of enzymes, their directed evolution and the engineering of (natural) metabolic pathways. In this work, the LuxAB biosensor system from Photorhabdus luminescens was implemented in Escherichia coli to monitor the enzymatic production of aldehydes from primary alcohols and carboxylic acid substrates. A simple high-throughput assay utilized the bacterial luciferase—previously reported to only accept aliphatic long-chain aldehydes—to detect structurally diverse aldehydes, including aromatic and monoterpene aldehydes. LuxAB was used to screen the substrate scopes of three prokaryotic oxidoreductases: an alcohol dehydrogenase (Pseudomonas putida), a choline oxidase variant (Arthrobacter chlorophenolicus) and a carboxylic acid reductase (Mycobacterium marinum). Consequently, high-value aldehydes such as cinnamaldehyde, citral and citronellal could be produced in vivo in up to 80% yield. Furthermore, the dual role of LuxAB as sensor and monooxygenase, emitting bioluminescence through the oxidation of aldehydes to the corresponding carboxylates, promises implementation in artificial enzyme cascades for the synthesis of carboxylic acids. These findings advance the bio-based detection, preparation and transformation of industrially important aldehydes in living cells. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions (in vivo and in vitro))
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8 pages, 1128 KiB  
Article
Chemo-Enzymatic Cascade for the Generation of Fragrance Aldehydes
by Daniel Schwendenwein, Anna K. Ressmann, Marcello Entner, Viktor Savic, Margit Winkler and Florian Rudroff
Catalysts 2021, 11(8), 932; https://doi.org/10.3390/catal11080932 - 30 Jul 2021
Cited by 5 | Viewed by 2831
Abstract
In this study, we present the synthesis of chiral fragrance aldehydes, which was tackled by a combination of chemo-catalysis and a multi-enzymatic in vivo cascade reaction and the development of a highly versatile high-throughput assay for the enzymatic reduction of carboxylic acids. We [...] Read more.
In this study, we present the synthesis of chiral fragrance aldehydes, which was tackled by a combination of chemo-catalysis and a multi-enzymatic in vivo cascade reaction and the development of a highly versatile high-throughput assay for the enzymatic reduction of carboxylic acids. We investigated a biocompatible metal-catalyzed synthesis for the preparation of α or β substituted cinnamic acid derivatives which were fed directly into the biocatalytic system. Subsequently, the target molecules were synthesized by an enzymatic cascade consisting of a carboxylate reduction, followed by the selective C-C double bond reduction catalyzed by appropriate enoate reductases. We investigated a biocompatible oxidative Heck protocol and combined it with cells expressing a carboxylic acid reductase from Neurospora crassa (NcCAR) and an ene reductase from Saccharomyces pastorianus for the production fragrance aldehydes. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions (in vivo and in vitro))
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