Dear Colleagues,

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
Guest Editors

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• acylation
• alcohols
• amines
• dynamic kinetic resolution
• esterases
• fine chemicals
• hydrolysis
• kinetic resolution
• lipases
• organic reaction media
• pharmaceutical products
• proteases
• β-amino acids
• CaL-B

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.