Biotransformation Catalyzed by Immobilized Enzyme

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

Deadline for manuscript submissions: closed (30 January 2022) | Viewed by 7527

Special Issue Editors


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Guest Editor
Biocatalysis & Organic Chemistry, Delft University of Technology, Delft, The Netherlands
Interests: enzymes that enable the formation of C–C bonds or catalyze reactions that are chemically extremely difficult to perform; their immobilization and application in organic synthesis

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Guest Editor
1. Biological & Food Engineering, University of Lorraine (UL), 54000 Nancy, France
2. The Reactions and Chemical Engineering Laboratory (LRGP), National Center for Scientific Research, 75016 Paris, France
Interests: enzymes, in particular aminoacylases for performing N-acylation reactions in aqueous phase, and lipases for performing O-acylation reactions in anhydrous solvents (supercritical CO2 or organic solvent)

Special Issue Information

Dear Colleagues,

It is our pleasure to invite you to contribute to this Special Issue of Catalysts, entitled “Biotransformations Catalyzed by Immobilized Enzymes”.

Biotransformations catalyzed by immobilized enzymes represent a fascinating research and development area. From studies in the laboratory via pilot scale-up to successfully implemented large- or very large-scale production in food, pharmaceutical, biofuel, and biodegradable plastics, immobilized enzymes catalyze a broad range of reactions.

Regardless of the immobilization strategy used, the targeted advantages of immobilization are:

(i)  Easy recovery/separation of the biocatalyst from the reaction mixture;

(ii)  Easy recycling through multiple runs;

(iii)  Improved stability (and sometimes activity) versus process parameters, such as temperature or pH;

(iv) Continuous flow reactors such as packed bed reactors in order to suppress inhibition of the enzyme by the reaction product(s) while getting full conversion and pure products in cases of equimolar ratio of substrates and where appropriate process conditions are used.

Combining these four advantages, region-, chemo- or enantio-selectivity of the immobilized enzymes can lead to single successful transformation or, even better, cascade biotransformation processes.

We therefore invite you to submit your current work in this area, but also in the adjacent fields such as:

(i)  Biotransformations catalyzed by immobilized enzymes in anhydrous solvent (organic, supercritical, eutectic, ionic);

(ii)  Use and up-scalability in a reactor and/or recyclability;

(iii) Process intensification involving immobilized enzymes;

(iv) Production cost and eco-compatibility (lifecycle assessments, etc.).

In this Special Issue, we welcome contributions from all aspects of biotransformations catalyzed by immobilized enzymes. The following keywords are a guideline: enzyme immobilization, enzyme recycling, enzyme carrier interaction, continuous reactions, biocatalytic cascades, non-aqueous reaction systems, downstream processing, lifecycle assessment.

We look forward to your contributions to this interesting field.

Prof. Dr. Ulf Hanefeld
Dr. Yann P. Guiavarc'h
Guest Editors

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Keywords

  • Enzyme immobilization
  • Enzyme recycling
  • Enzyme carrier interaction
  • Continuous reactions
  • Biocatalytic cascades
  • Non-aqueous reaction systems
  • Downstream processing
  • Lifecycle assessment

Published Papers (3 papers)

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Research

23 pages, 3925 KiB  
Article
The Effect of pH, Metal Ions, and Insoluble Solids on the Production of Fumarate and Malate by Rhizopus delemar in the Presence of CaCO3
by Dominic Kibet Ronoh, Reuben Marc Swart, Willie Nicol and Hendrik Brink
Catalysts 2022, 12(3), 263; https://doi.org/10.3390/catal12030263 - 25 Feb 2022
Cited by 2 | Viewed by 2013
Abstract
Calcium carbonate has been extensively used as a neutralising agent in acid-forming microbial processes. The effect of increasing calcium carbonate concentrations on Rhizopus delemar has not been previously investigated. In this study, an evaluation of fumaric acid (FA) and malic acid (MA) production [...] Read more.
Calcium carbonate has been extensively used as a neutralising agent in acid-forming microbial processes. The effect of increasing calcium carbonate concentrations on Rhizopus delemar has not been previously investigated. In this study, an evaluation of fumaric acid (FA) and malic acid (MA) production was conducted at three CaCO3 concentrations in shake flask cultivations. Increased CaCO3 concentrations resulted in the co-production of FA and MA in the first 55 h of the fermentation (regime 1), and the subsequent depletion of FA thereafter (regime 2). Three factors were highlighted as likely causes of this response: insoluble solids, metal ion concentrations, and pH. Further shake flask cultivations as well as a continuous fermentation with immobilised R. delemar were used to explore the effect of the three factors on regime 1 and 2. Insoluble solids were found to have no effect on the response in either regime 1 or 2. Increasing the aqueous calcium ion concentrations to 10 g L−1 resulted in a three-fold increase in MA titres (regime 1). Moreover, an increase in pH above 7 was associated with a drop in FA concentrations in regime 2. Further tests established that this was due to the hydration of FA to MA, influenced by high pH conditions (7 or higher), nitrogen starvation, and glucose depletion. Anaerobic conditions were also found to significantly improve the hydration process. This study presents the first investigation in which the production of FA followed by in situ hydration of FA to MA with R. delemar has been achieved. Full article
(This article belongs to the Special Issue Biotransformation Catalyzed by Immobilized Enzyme)
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12 pages, 798 KiB  
Article
Batch and Flow Nitroaldol Synthesis Catalysed by Granulicella tundricola Hydroxynitrile Lyase Immobilised on Celite R-633
by José Coloma, Lidwien Teeuwisse, Muhammad Afendi, Peter-Leon Hagedoorn and Ulf Hanefeld
Catalysts 2022, 12(2), 161; https://doi.org/10.3390/catal12020161 - 27 Jan 2022
Cited by 4 | Viewed by 2229
Abstract
Granulicella tundricola hydroxynitrile lyase (GtHNL) catalyses the synthesis of chiral (R)-cyanohydrins and (R)-β-nitro alcohols. The triple variant GtHNL-A40H/V42T/Q110H (GtHNL-3V) was immobilised on Celite R-633 and used in monophasic MTBE saturated with 100 mM KPi [...] Read more.
Granulicella tundricola hydroxynitrile lyase (GtHNL) catalyses the synthesis of chiral (R)-cyanohydrins and (R)-β-nitro alcohols. The triple variant GtHNL-A40H/V42T/Q110H (GtHNL-3V) was immobilised on Celite R-633 and used in monophasic MTBE saturated with 100 mM KPi buffer pH 7 for the synthesis of (R)-2-nitro-1-phenylethanol (NPE) in batch and continuous flow systems. Nitromethane was used as a nucleophile. A total of 82% of (R)-NPE and excellent enantioselectivity (>99%) were achieved in the batch system after 24 h of reaction time. GtHNL-3V on Celite R-633 was successfully recycled five times. During more recycling steps a significant decrease in yield was observed while the enantioselectivity remained excellent over eight cycles. The use of a flow system enabled the continuous synthesis of (R)-NPE. A total of 15% formation of (R)-NPE was reached using a flow rate of 0.1 mL min−1; unfortunately, the enzyme was not stable, and the yield decreased to 4% after 4 h on stream. A similar yield was observed during 15 h at a rate of 0.01 mL min−1. Surprisingly the use of a continuous flow system did not facilitate the process intensification. In fact, the batch system displayed a space-time-yield (STY/mgenzyme) of 0.10 g L−1 h−1 mgenzyme−1 whereas the flow system displayed 0.02 and 0.003 g L−1 h−1 mgenzyme−1 at 0.1 and 0.01 mL min−1, respectively. In general, the addition of 1 M nitromethane potentially changed the polarity of the reaction mixture affecting the stability of Celite-GtHNL-3V. The nature of the batch system maintained the reaction conditions better than the flow system. The higher yield and productivity observed for the batch system show that it is a superior system for the synthesis of (R)-NPE compared with the flow approach. Full article
(This article belongs to the Special Issue Biotransformation Catalyzed by Immobilized Enzyme)
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13 pages, 3219 KiB  
Article
Continuous Diastereomeric Kinetic Resolution—Silybins A and B
by David Biedermann, Martina Hurtová, Oldřich Benada, Kateřina Valentová, Lada Biedermannová and Vladimír Křen
Catalysts 2021, 11(9), 1106; https://doi.org/10.3390/catal11091106 - 14 Sep 2021
Cited by 4 | Viewed by 2255
Abstract
The natural diastereomeric mixture of silybins A and B is often used (and considered) as a single flavonolignan isolated from the fruit extract of milk thistle (Silybum marianum), silymarin. However, optically pure silybin diastereomers are required for the evaluation of their [...] Read more.
The natural diastereomeric mixture of silybins A and B is often used (and considered) as a single flavonolignan isolated from the fruit extract of milk thistle (Silybum marianum), silymarin. However, optically pure silybin diastereomers are required for the evaluation of their biological activity. The separation of silybin diastereomers by standard chromatographic methods is not trivial. Preparative chemoenzymatic resolution of silybin diastereomers has been published, but its optimization and scale-up are needed. Here we present a continuous flow reactor for the chemoenzymatic kinetic resolution of silybin diastereomers catalyzed by Candida antarctica lipase B (CALB) immobilized on acrylic resin beads (Novozym® 435). Temperature, flow rate, and starting material concentration were varied to determine optimal reaction conditions. The variables observed were conversion and diastereomeric ratio. Optimal conditions were chosen to allow kilogram-scale reactions and were determined to be −5 °C, 8 g/L silybin, and a flow rate of 16 mL/min. No significant carrier degradation was observed after approximately 30 cycles (30 days). Under optimal conditions and using a 1000 × 15 mm column, 20 g of silybin per day can be easily processed, yielding 6.7 and 5.6 g of silybin A and silybin B, respectively. Further scale-up depends only on the size of the reactor. Full article
(This article belongs to the Special Issue Biotransformation Catalyzed by Immobilized Enzyme)
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