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Molecules
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Frontier in Biocatalysis for Organic Synthesis
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Frontier in Biocatalysis for Organic Synthesis

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (20 July 2018) | Viewed by 26598

Special Issue Editors

Prof. Dr. Frank Hollmann

E-Mail Website
Guest Editor
Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629HZ Delft, The Netherlands
Interests: biocatalysis; oxidation chemistry; oxyfunctionalisation reactions; green chemistry
Dr. Selin Kara

E-Mail Website
Guest Editor
Institute of Technical Biocatalysis, Hamburg University of Technology, Denickestr. 15, 21075 Hamburg, Germany
Interests: biocatalytic cascade reactions; redox biocatalysis; biocatalysis in non-conventional media; enzyme immobilization; reaction engineering
Dr. Caroline E. Paul

E-Mail Website
Guest Editor
Laboratory of Organic Chemistry, Wageningen University & Research, Stippeneng 4, 6708WE Wageningen, The Netherlands
Interests: biocatalysis; oxidoreductases; nicotinamide cofactors; synthetic coenzyme biomimetics; redox reactions

Special Issue Information

Dear Colleagues,

The importance of biocatalysis for organic synthesis is steadily growing. Already, enzymes are used by various chemical industries, but their potential is not yet fully tapped. Biocatalytic methods can give an alternative or complementary route in classical organic synthesis. An increasing number of biocatalytic processes, such as enzymatic cascades and hydrogen-borrowing systems, are being developed with new enzyme reactivity still being discovered. Spatial arrangements in multi-enzymatic systems via compartmentalization or co-immobilization of enzymes have been a useful tool to increase productivities.

In this Special Issue we aim to compile contributions from academic research and industrial application to showcase the potential, but also the current limitations of biocatalysis for organic synthesis.

Manuscripts describing new enzymatic reactions for organic synthesis, as well as manuscripts dealing with improved enzymatic processes based on engineered enzymes, optimized biocatalyst formulations, and/or engineered reaction setups are very welcome.

Dr. Frank Hollmann
Dr. Selin Kara
Dr. Caroline E. Paul
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. Molecules is an international peer-reviewed open access semimonthly 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 for organic chemistry
  • biotransformations
  • (multi-step) enzymatic reactions
  • organic synthesis
  • spatial arrangements in enzymatic cascades
  • biocatalyst formulation for enzymatic synthesis
  • reaction engineering in biocatalytic systems

Published Papers (4 papers)

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Research

16 pages, 3747 KiB  
Article
Influence of Glutaraldehyde Cross-Linking Modes on the Recyclability of Immobilized Lipase B from Candida antarctica for Transesterification of Soy Bean Oil
by Iago A. Modenez, Diego E. Sastre, Fernando C. Moraes and Caterina G. C. Marques Netto
Molecules 2018, 23(9), 2230; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules23092230 - 02 Sep 2018
Cited by 33 | Viewed by 9081
Abstract
Lipase B from Candida antarctica (CAL-B) is largely employed as a biocatalyst for hydrolysis, esterification, and transesterification reactions. CAL-B is a good model enzyme to study factors affecting the enzymatic structure, activity and/or stability after an immobilization process. In this study, we analyzed [...] Read more.
Lipase B from Candida antarctica (CAL-B) is largely employed as a biocatalyst for hydrolysis, esterification, and transesterification reactions. CAL-B is a good model enzyme to study factors affecting the enzymatic structure, activity and/or stability after an immobilization process. In this study, we analyzed the immobilization of CAL-B enzyme on different magnetic nanoparticles, synthesized by the coprecipitation method inside inverse micelles made of zwitterionic surfactants, with distinct carbon chain length: 4 (ImS4), 10 (ImS10) and 18 (ImS18) carbons. Magnetic nanoparticles ImS4 and ImS10 were shown to cross-link to CAL-B enzyme via a Michael-type addition, whereas particles with ImS18 were bond via pyridine formation after glutaraldehyde cross-coupling. Interestingly, the Michael-type cross-linking generated less stable immobilized CAL-B, revealing the influence of a cross-linking mode on the resulting biocatalyst behavior. Curiously, a direct correlation between nanoparticle agglomerate sizes and CAL-B enzyme reuse stability was observed. Moreover, free CAL-B enzyme was not able to catalyze transesterification due to the high methanol concentration; however, the immobilized CAL-B enzyme reached yields from 79.7 to 90% at the same conditions. In addition, the transesterification of lipids isolated from oleaginous yeasts achieved 89% yield, which confirmed the potential of immobilized CAL-B enzyme in microbial production of biodiesel. Full article
(This article belongs to the Special Issue Frontier in Biocatalysis for Organic Synthesis)
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11 pages, 1073 KiB  
Communication
β-Phenylalanine Ester Synthesis from Stable β-Keto Ester Substrate Using Engineered ω-Transaminases
by Oliver Buß, Moritz Voss, André Delavault, Pascal Gorenflo, Christoph Syldatk, Uwe Bornscheuer and Jens Rudat
Molecules 2018, 23(5), 1211; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules23051211 - 18 May 2018
Cited by 14 | Viewed by 6764
Abstract
The successful synthesis of chiral amines from ketones using ω-transaminases has been shown in many cases in the last two decades. In contrast, the amination of β-keto acids is a special and relatively new challenge, as they decompose easily in aqueous solution. To [...] Read more.
The successful synthesis of chiral amines from ketones using ω-transaminases has been shown in many cases in the last two decades. In contrast, the amination of β-keto acids is a special and relatively new challenge, as they decompose easily in aqueous solution. To avoid this, transamination of the more stable β-keto esters would be an interesting alternative. For this reason, ω-transaminases were tested in this study, which enabled the transamination of the β-keto ester substrate ethyl benzoylacetate. Therefore, a ω-transaminase library was screened using a coloring o-xylylenediamine assay. The ω-transaminase mutants 3FCR_4M and ATA117 11Rd show great potential for further engineering experiments aiming at the synthesis of chiral (S)- and (R)-β-phenylalanine esters. This alternative approach resulted in the conversion of 32% and 13% for the (S)- and (R)-enantiomer, respectively. Furthermore, the (S)-β-phenylalanine ethyl ester was isolated by performing a semi-preparative synthesis. Full article
(This article belongs to the Special Issue Frontier in Biocatalysis for Organic Synthesis)
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15 pages, 4016 KiB  
Article
Efficient (3S)-Acetoin and (2S,3S)-2,3-Butanediol Production from meso-2,3-Butanediol Using Whole-Cell Biocatalysis
by Yuanzhi He, Feixue Chen, Meijing Sun, Huifang Gao, Zewang Guo, Hui Lin, Jiebo Chen, Wensong Jin, Yunlong Yang, Liaoyuan Zhang and Jun Yuan
Molecules 2018, 23(3), 691; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules23030691 - 19 Mar 2018
Cited by 28 | Viewed by 5213
Abstract
(3S)-Acetoin and (2S,3S)-2,3-butanediol are important platform chemicals widely applied in the asymmetric synthesis of valuable chiral chemicals. However, their production by fermentative methods is difficult to perform. This study aimed to develop a whole-cell biocatalysis strategy for [...] Read more.
(3S)-Acetoin and (2S,3S)-2,3-butanediol are important platform chemicals widely applied in the asymmetric synthesis of valuable chiral chemicals. However, their production by fermentative methods is difficult to perform. This study aimed to develop a whole-cell biocatalysis strategy for the production of (3S)-acetoin and (2S,3S)-2,3-butanediol from meso-2,3-butanediol. First, E. coli co-expressing (2R,3R)-2,3-butanediol dehydrogenase, NADH oxidase and Vitreoscilla hemoglobin was developed for (3S)-acetoin production from meso-2,3-butanediol. Maximum (3S)-acetoin concentration of 72.38 g/L with the stereoisomeric purity of 94.65% was achieved at 24 h under optimal conditions. Subsequently, we developed another biocatalyst co-expressing (2S,3S)-2,3-butanediol dehydrogenase and formate dehydrogenase for (2S,3S)-2,3-butanediol production from (3S)-acetoin. Synchronous catalysis together with two biocatalysts afforded 38.41 g/L of (2S,3S)-butanediol with stereoisomeric purity of 98.03% from 40 g/L meso-2,3-butanediol. These results exhibited the potential for (3S)-acetoin and (2S,3S)-butanediol production from meso-2,3-butanediol as a substrate via whole-cell biocatalysis. Full article
(This article belongs to the Special Issue Frontier in Biocatalysis for Organic Synthesis)
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12 pages, 1755 KiB  
Article
Lipase-Catalyzed Acidolysis of Egg-Yolk Phosphatidylcholine with Citronellic Acid. New Insight into Synthesis of Isoprenoid-Phospholipids
by Magdalena Rychlicka, Natalia Niezgoda and Anna Gliszczyńska
Molecules 2018, 23(2), 314; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules23020314 - 02 Feb 2018
Cited by 15 | Viewed by 4931
Abstract
The development of a biotechnological method for the production of new biologically active phosphatidylcholine containing monoterpene citronellic acid (CA) was the aim of this work. Incorporation of citronellic acid (CA) into egg-yolk phosphatidylcholine (PC) in the lipase-catalyzed acidolysis process was studied. Isoprenoid acid [...] Read more.
The development of a biotechnological method for the production of new biologically active phosphatidylcholine containing monoterpene citronellic acid (CA) was the aim of this work. Incorporation of citronellic acid (CA) into egg-yolk phosphatidylcholine (PC) in the lipase-catalyzed acidolysis process was studied. Isoprenoid acid CA was used as an acyl donor and five commercially available immobilized lipases were examined as biocatalysts. The effects of organic solvent, enzyme load, reaction time and molar ratio of substrates on the incorporation of citronellic acid (CA) into the phospholipids were evaluated. Modified phospholipid fraction enriched with CA in the sn-1 position (39% of incorporation) was obtained in high 33% yield using Novozym 435 as biocatalyst. In this study a biotechnological method for production of new phospholipid biopreparation enriched with citronellic acid, which can play an important role as a nutraceutical, was applied. Full article
(This article belongs to the Special Issue Frontier in Biocatalysis for Organic Synthesis)
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