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Catalysts
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Enzyme-Mediated Stereoselective Synthesis II
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Enzyme-Mediated Stereoselective Synthesis II

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

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 9083

Special Issue Editor

Prof. Dr. Stefano Serra

E-Mail Website
Guest Editor
Consiglio Nazionale delle Ricerche (C.N.R.), Istituto di Scienze e Tecnologie Chimiche (SCITEC), Milano, Italy
Interests: organic synthesis; stereoselective synthesis; development of new synthetic methods; biotransformations and use of enzymes in organic synthesis; biogeneration of flavours and fragrances; natural products; synthesis and chemical characterization of APIs; antibiotics and biological active compounds
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The Special Issue is a continuation of the previous successful Special Issue "Enzyme-Mediated Stereoselective Synthesis".

All of us know very well the importance of catalysis in organic synthesis. Catalyzed reactions are usually preferred when planning a new synthetic approach, and the choice of the proper catalyst is of pivotal relevance.

In this context, the use of biocatalysts in organic synthesis has grown steadily during the last 50 years. Nowadays, chemists have become accustomed to the idea that the use of enzymes is essential in a modern synthetic laboratory. It does not matter if a given transformation is performed using whole cell microorganisms or using an isolated enzyme. In both cases, the specific activity and selectivity of one or more enzymes is exploited. In fact, biocatalysts allow for performing a number of chemical reactions with high regio- and stereoselectivity.

This second Special Issue on Enzyme-Mediated Stereoselective Synthesis has been planned in order to collect original research papers, reviews, and commentaries focused on the exploitation of enzyme stereoselectivity in organic synthesis. Contributions dealing with enzyme-mediated stereoselective synthesis of relevant chemicals, such as innovative materials; active pharmaceutical ingredients; natural products, flavors, and fragrances; and any other kind of bioactive compounds, are welcome.

Prof. Dr. Stefano Serra
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 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

  • Stereoselective synthesis
  • Enzymes in organic synthesis
  • Enantioselectivity
  • Diastereoselectivity
  • Biocatalysis
  • Enzyme-mediated resolution of racemic compounds
  • Whole-cells biocatalysis
  • Green chemistry

Published Papers (3 papers)

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Research

15 pages, 2366 KiB  
Article
Efficient 1-Hydroxy-2-Butanone Production from 1,2-Butanediol by Whole Cells of Engineered E. coli
by Hui Lin, Jiayin Xu, Wenlian Sun, Wujia Hu, Huifang Gao, Kaihui Hu, Junzhi Qiu, Binbin Huang and Liaoyuan Zhang
Catalysts 2021, 11(10), 1184; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11101184 - 28 Sep 2021
Cited by 5 | Viewed by 2351
Abstract
1-Hydroxy-2-butanone (HB) is a key intermediate for anti-tuberculosis pharmaceutical ethambutol. Commercially available HB is primarily obtained by the oxidation of 1,2-butanediol (1,2-BD) using chemical catalysts. In present study, seven enzymes including diol dehydrogenases, secondary alcohol dehydrogenases and glycerol dehydrogenase were chosen to evaluate [...] Read more.
1-Hydroxy-2-butanone (HB) is a key intermediate for anti-tuberculosis pharmaceutical ethambutol. Commercially available HB is primarily obtained by the oxidation of 1,2-butanediol (1,2-BD) using chemical catalysts. In present study, seven enzymes including diol dehydrogenases, secondary alcohol dehydrogenases and glycerol dehydrogenase were chosen to evaluate their abilities in the conversion of 1,2-BD to HB. The results showed that (2R, 3R)- and (2S, 3S)-butanediol dehydrogenase (BDH) from Serratia sp. T241 could efficiently transform (R)- and (S)-1,2-BD into HB respectively. Furthermore, two biocatalysts co-expressing (2R, 3R)-/(2S, 3S)-BDH, NADH oxidase and hemoglobin protein in Escherichia coli were developed to convert 1,2-BD mixture into HB, and the transformation conditions were optimized. Maximum HB yield of 341.35 and 188.80 mM could be achieved from 440 mM (R)-1,2-BD and 360 mM (S)-1,2-BD by E. coli (pET-rrbdh-nox-vgb) and E. coli (pET-ssbdh-nox-vgb) under the optimized conditions. In addition, two biocatalysts showed the ability in chiral resolution of 1,2-BD isomers, and 135.68 mM (S)-1,2-BD and 112.43 mM (R)-1,2-BD with the purity of 100% could be obtained from 300 and 200 mM 1,2-BD mixture by E. coli (pET-rrbdh-nox-vgb) and E. coli (pET-ssbdh-nox-vgb), respectively. These results provided potential application for HB production from 1,2-BD mixture and chiral resolution of (R)-1,2-BD and (S)-1,2-BD. Full article
(This article belongs to the Special Issue Enzyme-Mediated Stereoselective Synthesis II)
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14 pages, 1649 KiB  
Article
Oleate Hydratase from Lactobacillus rhamnosus ATCC 53103: A FADH2-Dependent Enzyme with Remarkable Industrial Potential
by Stefano Serra, Davide De Simeis, Stefano Marzorati and Mattia Valentino
Catalysts 2021, 11(9), 1051; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11091051 - 30 Aug 2021
Cited by 9 | Viewed by 3069
Abstract
Recently, we described the preparation of the recombinant oleate hydratase from Lactobacillus rhamnosus ATCC 53103. We observed that the purified C-terminal His-tagged enzyme was completely inactive and the catalytic activity was partially restored only in presence of a large amount of flavin adenine [...] Read more.
Recently, we described the preparation of the recombinant oleate hydratase from Lactobacillus rhamnosus ATCC 53103. We observed that the purified C-terminal His-tagged enzyme was completely inactive and the catalytic activity was partially restored only in presence of a large amount of flavin adenine dinucleotide (FAD). In the present work, we assess that this hydratase in the presence of the reduced form of flavin adenine dinucleotide (FADH2) is at least one hundred times as active as in the presence of the same concentration of FAD. By means of two different biochemical processes, we demonstrated unambiguously that oleate hydratase from Lactobacillus rhamnosus ATCC 53103 is a FADH2-dependent enzyme. As a first relevant application of this discovery, we devised a preparative procedure for the stereoselective synthesis of (R)-10-hydroxystearic acid. Accordingly, the hydration of oleic acid (up to 50 g/L) is performed on a multigram scale using the recombinant hydratase and FADH2 generated in situ as cofactor. The produced (R)-10-hydroxystearic acid (ee > 97%) precipitates from the reaction solvent (water/glycerol/ethanol) and is conveniently recovered by simple filtration (>90% yield). Full article
(This article belongs to the Special Issue Enzyme-Mediated Stereoselective Synthesis II)
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16 pages, 1021 KiB  
Article
Recombinant Oleate Hydratase from Lactobacillus rhamnosus ATCC 53103: Enzyme Expression and Design of a Reliable Experimental Procedure for the Stereoselective Hydration of Oleic Acid
by Antonio Castagna, Davide De Simeis, Erica E. Ferrandi, Stefano Marzorati, Daniela Monti, Stefano Serra and Mattia Valentino
Catalysts 2020, 10(10), 1122; https://0-doi-org.brum.beds.ac.uk/10.3390/catal10101122 - 01 Oct 2020
Cited by 7 | Viewed by 2949
Abstract
Different microbial strains are able to transform oleic acid (OA) into 10-hydroxystearic acid (10-HSA) by means of the catalytic activity of the enzymes oleate hydratase (EC 4.2.1.53). Lactobacillus rhamnosus ATCC 53103 performs this biotransformation with very high stereoselectivity, affording enantiopure (R)-10-HSA. [...] Read more.
Different microbial strains are able to transform oleic acid (OA) into 10-hydroxystearic acid (10-HSA) by means of the catalytic activity of the enzymes oleate hydratase (EC 4.2.1.53). Lactobacillus rhamnosus ATCC 53103 performs this biotransformation with very high stereoselectivity, affording enantiopure (R)-10-HSA. In this work, we cloned, in Escherichia coli, the oleate hydratase present in the above-mentioned probiotic strain. Our study demonstrated that the obtained recombinant hydratase retains the catalytic properties of the Lactobacillus strain but that its activity was greatly affected by the expression procedure. According to our findings, we devised a reliable procedure for the hydration of oleic acid using a recombinant E. coli whole-cell catalyst. We established that the optimal reaction conditions were pH 6.6 at 28 °C in phosphate buffer, using glycerol and ethanol as co-solvents. According to our experimental protocol, the biocatalyst does not show significant substrate inhibition as the hydration reaction can be performed at high oleic acid concentration (up to 50 g/L). Full article
(This article belongs to the Special Issue Enzyme-Mediated Stereoselective Synthesis II)
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