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Catalysts
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Flow Biocatalysis
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Flow Biocatalysis

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

Deadline for manuscript submissions: closed (31 January 2019) | Viewed by 40330

Special Issue Editor

Prof. Dr. Francesca Paradisi

E-Mail Website
Guest Editor
School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK
Interests: enzyme discovery, enzyme engineering, transaminases, ketoreductases, hydrolases, biocatalysis, flow-biocatalysis, efficiency in biotransformations, multi-enzymatic cascades

Special Issue Information

Dear Colleagues,

Flow-biocatalyisis is a very powerful technique which combines the power and advantages of enzymes with the high throughput of continuous synthesis. Assembly of multi-enzymatic systems either as immobilized whole cell factories, or immobilized cell-free enzymatic preparations, have been very successful in the synthesis of complex molecules with very high efficiency, mimicking, in some cases, biosynthetic pathways. Flow-biocatalysis encompasses a variety of techniques and can be easily combined with chemical steps, increasing the versatility of the reactor. This special issue collects original research papers, reviews and commentaries focused on novel biotransformations being carried out in continuous, with particular attention to the efficiency of the system. Submissions are welcome in all areas of flow-biocatalysis:

  • Cell-free immobilized enzymes;
  • Whole cells immobilized systems;
  • Multi-enzymatic reactions in flow;
  • Methods of immobilizations of the biocatalysts to improve durability;
  • Chemo-enzymatic continuous processes;
  • Cofactor-recycling;
  • Co-immobilization of enzymes;
  • Downstream purification methods;
  • In-line reaction monitoring;
  • 3D-printed reactors for flow-biocatalysis.
Prof. Dr. Francesca Paradisi
Guest Editor

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 2200 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

  • Biotransformations
  • Flow-biocatalysis
  • Downstream processing
  • Enzyme preparation
  • Chemocatalysis
  • Operational stability

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Published Papers (6 papers)

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Editorial

Jump to: Research, Review

2 pages, 156 KiB  
Editorial
Flow Biocatalysis
by Francesca Paradisi
Catalysts 2020, 10(6), 645; https://doi.org/10.3390/catal10060645 - 9 Jun 2020
Cited by 7 | Viewed by 1918
Abstract
The rapid evolution of enzyme technology has enabled new reactions and processes with a level of efficiency which was unimaginable only a few years ago [...] Full article
(This article belongs to the Special Issue Flow Biocatalysis)

Research

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11 pages, 943 KiB  
Article
Immobilized Whole-Cell Transaminase Biocatalysts for Continuous-Flow Kinetic Resolution of Amines
by Zsófia Molnár, Emese Farkas, Ágnes Lakó, Balázs Erdélyi, Wolfgang Kroutil, Beáta G. Vértessy, Csaba Paizs and László Poppe
Catalysts 2019, 9(5), 438; https://doi.org/10.3390/catal9050438 - 10 May 2019
Cited by 34 | Viewed by 7064
Abstract
Immobilization of transaminases creates promising biocatalysts for production of chiral amines in batch or continuous-flow mode reactions. E. coli cells containing overexpressed transaminases of various selectivities and hollow silica microspheres as supporting agent were immobilized by an improved sol-gel process to produce immobilized [...] Read more.
Immobilization of transaminases creates promising biocatalysts for production of chiral amines in batch or continuous-flow mode reactions. E. coli cells containing overexpressed transaminases of various selectivities and hollow silica microspheres as supporting agent were immobilized by an improved sol-gel process to produce immobilized transaminase biocatalysts with suitable stability and mechanical properties for continuous-flow applications. The immobilized cell-based transaminase biocatalyst proved to be durable and easy-to-use in kinetic resolution of four racemic amines 1a–d. The batch and continuous-flow mode kinetic resolutions with transaminase biocatalyst of opposite stereopreference provided access to both enantiomers of the corresponding amines. By using the most suitable immobilized transaminase biocatalysts, this study describes the first transaminase-based approach for the production of both pure enantiomers of 1-(3,4-dimethoxyphenyl)ethan-1-amine 1d. Full article
(This article belongs to the Special Issue Flow Biocatalysis)
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10 pages, 3527 KiB  
Article
Overcoming Water Insolubility in Flow: Enantioselective Hydrolysis of Naproxen Ester
by David Roura Padrosa, Valerio De Vitis, Martina Letizia Contente, Francesco Molinari and Francesca Paradisi
Catalysts 2019, 9(3), 232; https://doi.org/10.3390/catal9030232 - 3 Mar 2019
Cited by 19 | Viewed by 4578
Abstract
Hydrolytic enantioselective cleavage of different racemic non-steroidal anti-inflammatory drugs (NSAIDs) ester derivatives has been studied. An engineered esterase form Bacillus subtilis (BS2m) significantly outperformed homologous enzymes from Halomonas elongata (HeE) and Bacillus coagulants (BCE) in the enantioselective hydrolysis of naproxen esters. Structural analysis [...] Read more.
Hydrolytic enantioselective cleavage of different racemic non-steroidal anti-inflammatory drugs (NSAIDs) ester derivatives has been studied. An engineered esterase form Bacillus subtilis (BS2m) significantly outperformed homologous enzymes from Halomonas elongata (HeE) and Bacillus coagulants (BCE) in the enantioselective hydrolysis of naproxen esters. Structural analysis of the three active sites highlighted key differences which explained the substrate preference. Immobilization of a chimeric BS2m-T4 lysozyme fusion (BS2mT4L1) was improved by resin screening achieving twice the recovered activity (22.1 ± 5 U/g) with respect to what had been previously reported, and was utilized in a packed bed reactor. Continuous hydrolysis of α-methyl benzene acetic acid butyl ester as a model substrate was easily achieved, albeit at low concentration (1 mM). However, the high degree of insolubility of the naproxen butyl ester resulted in a slurry which could not be efficiently bioconverted, despite the addition of co-solvents and lower substrate concentration (1 mM). Addition of Triton® X-100 to the substrate mix yielded 24% molar conversion and 80% e.e. at a 5 mM scale with 5 min residence time and sufficient retention of catalytic efficiency after 6 h of use. Full article
(This article belongs to the Special Issue Flow Biocatalysis)
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10 pages, 1404 KiB  
Article
Bioprocess Intensification Using Flow Reactors: Stereoselective Oxidation of Achiral 1,3-diols with Immobilized Acetobacter Aceti
by Valerio De Vitis, Federica Dall’Oglio, Francesca Tentori, Martina Letizia Contente, Diego Romano, Elisabetta Brenna, Lucia Tamborini and Francesco Molinari
Catalysts 2019, 9(3), 208; https://doi.org/10.3390/catal9030208 - 26 Feb 2019
Cited by 22 | Viewed by 4054
Abstract
Enantiomerically enriched 2-hydroxymethylalkanoic acids were prepared by oxidative desymmetrisation of achiral 1,3-diols using immobilized cells of Acetobacter aceti in water at 28 °C. The biotransformations were first performed in batch mode with cells immobilized in dry alginate, furnishing the desired products with high [...] Read more.
Enantiomerically enriched 2-hydroxymethylalkanoic acids were prepared by oxidative desymmetrisation of achiral 1,3-diols using immobilized cells of Acetobacter aceti in water at 28 °C. The biotransformations were first performed in batch mode with cells immobilized in dry alginate, furnishing the desired products with high molar conversion and reaction times ranging from 2 to 6 h. The biocatalytic process was intensified using a multiphasic flow reactor, where a segmented gas–liquid flow regime was applied for achieving an efficient O2-liquid transfer; the continuous flow systems allowed for high yields and high biocatalyst productivity. Full article
(This article belongs to the Special Issue Flow Biocatalysis)
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13 pages, 2841 KiB  
Article
Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors
by Theo Peschke, Patrick Bitterwolf, Silla Hansen, Jannis Gasmi, Kersten S. Rabe and Christof M. Niemeyer
Catalysts 2019, 9(2), 164; https://doi.org/10.3390/catal9020164 - 8 Feb 2019
Cited by 23 | Viewed by 7427
Abstract
Maximizing space–time yields (STY) of biocatalytic flow processes is essential for the establishment of a circular biobased economy. We present a comparative study in which different biocatalytic flow reactor concepts were tested with the same enzyme, the (R)-selective alcohol dehydrogenase from [...] Read more.
Maximizing space–time yields (STY) of biocatalytic flow processes is essential for the establishment of a circular biobased economy. We present a comparative study in which different biocatalytic flow reactor concepts were tested with the same enzyme, the (R)-selective alcohol dehydrogenase from Lactobacillus brevis (LbADH), that was used for stereoselective reduction of 5-nitrononane-2,8-dione. The LbADH contained a genetically encoded streptavidin (STV)-binding peptide to enable self-immobilization on STV-coated surfaces. The purified enzyme was immobilized by physisorption or chemisorption as monolayers on the flow channel walls, on magnetic microbeads in a packed-bed format, or as self-assembled all-enzyme hydrogels. Moreover, a multilayer biofilm with cytosolic-expressed LbADH served as a whole-cell biocatalyst. To enable cross-platform comparison, STY values were determined for the various reactor modules. While mono- and multilayer coatings of the reactor surface led to STY < 10, higher productivity was achieved with packed-bed reactors (STY ≈ 100) and the densely packed hydrogels (STY > 450). The latter modules could be operated for prolonged times (>6 days). Given that our approach should be transferable to other enzymes, we anticipate that compartmentalized microfluidic reaction modules equipped with self-immobilizing biocatalysts would be of great utility for numerous biocatalytic and even chemo-enzymatic cascade reactions under continuous flow conditions. Full article
(This article belongs to the Special Issue Flow Biocatalysis)
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Review

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17 pages, 2200 KiB  
Review
Reactor Selection for Effective Continuous Biocatalytic Production of Pharmaceuticals
by Rowan M. Lindeque and John M. Woodley
Catalysts 2019, 9(3), 262; https://doi.org/10.3390/catal9030262 - 14 Mar 2019
Cited by 70 | Viewed by 14077
Abstract
Enzyme catalyzed reactions are rapidly becoming an invaluable tool for the synthesis of many active pharmaceutical ingredients. These reactions are commonly performed in batch, but continuous biocatalysis is gaining interest in industry because it would allow seamless integration of chemical and enzymatic reaction [...] Read more.
Enzyme catalyzed reactions are rapidly becoming an invaluable tool for the synthesis of many active pharmaceutical ingredients. These reactions are commonly performed in batch, but continuous biocatalysis is gaining interest in industry because it would allow seamless integration of chemical and enzymatic reaction steps. However, because this is an emerging field, little attention has been paid towards the suitability of different reactor types for continuous biocatalytic reactions. Two types of continuous flow reactor are possible: continuous stirred tank and continuous plug-flow. These reactor types differ in a number of ways, but in this contribution, we focus on residence time distribution and how enzyme kinetics are affected by the unique mass balance of each reactor. For the first time, we present a tool to facilitate reactor selection for continuous biocatalytic production of pharmaceuticals. From this analysis, it was found that plug-flow reactors should generally be the system of choice. However, there are particular cases where they may need to be coupled with a continuous stirred tank reactor or replaced entirely by a series of continuous stirred tank reactors, which can approximate plug-flow behavior. This systematic approach should accelerate the implementation of biocatalysis for continuous pharmaceutical production. Full article
(This article belongs to the Special Issue Flow Biocatalysis)
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