Special Issue "Enzyme-Mediated Stereoselective Synthesis"

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: 31 July 2018

Special Issue Editor

Guest Editor
Dr. Stefano Serra

C.N.R. Istituto di Chimica del Riconoscimento Molecolare, Via Mancinelli 7, I-20131 Milano, Italy
Website | E-Mail
Interests: organic synthesis; stereoselective synthesis, development of new synthetic methods; biotransformations and use of enzymes in organic synthesis; natural products; flavour and fragrance chemistry

Special Issue Information

Dear Colleagues,

All of us know very well the importance of the 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 fifty 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 performing a number of chemical reactions with high regio- and stereoselectivity.

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

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 1300 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 (2 papers)

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Research

Open AccessArticle Microbial Kinetic Resolution of Aroma Compounds Using Solid-State Fermentation
Catalysts 2018, 8(1), 28; doi:10.3390/catal8010028
Received: 14 December 2017 / Revised: 12 January 2018 / Accepted: 13 January 2018 / Published: 16 January 2018
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Abstract
A novel microbial approach to the production of enantiomerically enriched and pure aroma compounds based on kinetic resolution via solid-state fermentation is proposed. Twenty-five filamentous fungi were screened for lipase activity and enantioselective hydrolysis of a volatile racemic ester (1-phenylethyl acetate (1
[...] Read more.
A novel microbial approach to the production of enantiomerically enriched and pure aroma compounds based on kinetic resolution via solid-state fermentation is proposed. Twenty-five filamentous fungi were screened for lipase activity and enantioselective hydrolysis of a volatile racemic ester (1-phenylethyl acetate (1)) and several racemic lactones (trans and cis whisky lactones (4, 5), γ-decalactone (7), δ-decalactone (8), (cis-3a,4,7,7a-tetrahydro-1(3H)-isobenzofuranone) (9)). Solid-state fermentation was conducted with linseed and rapeseed cakes. Kinetic resolution afforded enantiomerically enriched products with high enantiomeric excesses (ee = 82–99%). The results highlight the potential economic value of solid-state fermentation using agroindustrial side-stream feedstocks as an alternative to more expensive processes conducted in submerged fermentation. Full article
(This article belongs to the Special Issue Enzyme-Mediated Stereoselective Synthesis)
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Open AccessArticle Immobilized Burkholderia cepacia Lipase on pH-Responsive Pullulan Derivatives with Improved Enantioselectivity in Chiral Resolution
Catalysts 2018, 8(1), 13; doi:10.3390/catal8010013
Received: 12 December 2017 / Revised: 5 January 2018 / Accepted: 5 January 2018 / Published: 9 January 2018
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Abstract
A kind of pH-responsive particle was synthesized using modified pullulan polysaccharide. The synthesized particle possessed a series of merits, such as good dispersity, chemical stability and variability of particle size, making it a suitable carrier for enzyme immobilization. Then, Burkholderia cepacia lipase (BCL),
[...] Read more.
A kind of pH-responsive particle was synthesized using modified pullulan polysaccharide. The synthesized particle possessed a series of merits, such as good dispersity, chemical stability and variability of particle size, making it a suitable carrier for enzyme immobilization. Then, Burkholderia cepacia lipase (BCL), a promising biocatalyst in transesterification reaction, was immobilized on the synthesized particle. The highest catalytic activity and immobilization efficiency were achieved at pH 6.5 because the particle size was obviously enlarged and correspondingly the adsorption surface for BCL was significantly increased. The immobilization enzyme loading was further optimized, and the derivative lipase was applied in chiral resolution. Under the optimal reaction conditions, the immobilized BCL showed a very good performance and significantly shortened the reaction equilibrium time from 30 h of the free lipase to 2 h with a conversion rate of 50.0% and ees at 99.2%. The immobilized lipase also exhibited good operational stability; after being used for 10 cycles, it still retained over 80% of its original activity. Moreover, it could keep more than 80% activity after storage for 20 days at room temperature in a dry environment. In addition, to learn the potential mechanism, the morphology of the particles and the immobilized lipase were both characterized with a scanning electron microscope and confocal laser scanning microscopy. It was found that the enlarged spherical surface of the particle in low pH values probably led to high immobilized efficiency, resulting in the improvement of enantioselectivity activity in chiral resolution. Full article
(This article belongs to the Special Issue Enzyme-Mediated Stereoselective Synthesis)
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