Special Issue "Biocatalytic Resolution of Chiral Molecules"
Deadline for manuscript submissions: 30 June 2021.
Interests: asymmetric synthesis of enantiopure compounds; synthesis and modification of peptides with properties in catalysis and medicinal chemistry; biocatalysis; sustainable chemistry (green chemistry); synthesis of heterocyclic compounds
Special Issues and Collections in MDPI journals
Special Issue in Catalysts: Multi-Step Syntheses in Biology & Chemistry
Interests: stereochemistry and conformational analysis; asymmetric synthesis; enantioselective organocatalysis; green chemistry
Natural catalysts such as enzymes often outperform synthetic catalysts, both kinetically and in terms of selectivity (e.g., enantioselectivity). Biocatalysis can usually be carried out under mild conditions (e.g., ambient temperature and pressure, aqueous and organic solutions), and the catalysts used are generally biodegradable, biocompatible, and renewable, making these catalytic systems highly attractive for environmentally benign processes. A major application of enzymes, which has already gained industrial importance, are kinetic resolutions of racemic substrates. What makes enzymatic resolution attractive is the easy access to racemic substrates by means of many chemical methodologies in combination with the high efficiency and selectivity provided by the biocatalyst. In spite of the achievements in these fields, numerous challenges still exist.
This Special Issue will discuss recent developments in the preparation of enantiopure substances by means of enantioselective enzymatic resolutions and will include strategies that involve enzymatic catalysis in combination with chemical, photochemical, mechanochemical, and other types of non-traditional activation. A further focus of this special Issue will also be on dynamic kinetic resolution processes combining enzymatic resolutions with novel types of chemocatalytic or enzymatic racemization steps.
Prof. Dr. Jaime Escalante
Prof. Dr. Harald Gröger
Prof. Dr. Eusebio Juaristi
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.
- dynamic kinetic resolution
- fine chemicals
- kinetic resolution
- organic reaction media
- pharmaceutical products
- β-amino acids
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Synthesis of Optically Active Piperidines Using Hydrolase
Authors: Koichi Mitsukura
Affiliation: Department of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University 1-1 Yanagido, Gifu 501-1193, Japan
Abstract: We have found a bacterium with an (S)-selective hydrolase that convert racemic N-acyl-2-methylpiperidine to (S)-2-methylpiperidine. In the present study, we describe the characterization and substrate specificity of the purified (S)-selective hydrolase.