Special Issue "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 March 2021).

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
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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 papers will be 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 2000 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.


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

Published Papers (1 paper)

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Recombinant Oleate Hydratase from Lactobacillus rhamnosus ATCC 53103: Enzyme Expression and Design of a Reliable Experimental Procedure for the Stereoselective Hydration of Oleic Acid
Catalysts 2020, 10(10), 1122; https://doi.org/10.3390/catal10101122 - 01 Oct 2020
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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 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 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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