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Developments and Advances in Biocatalysis of Chiral Drugs

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 20 February 2025 | Viewed by 1534

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Guest Editor
Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland
Interests: biocatalysis; chiral separation; enzyme; enzyme engineering; green chemistry; immobilization; kinetic resolution; support material modification
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Special Issue Information

Dear Colleagues,

In recent years, an intensively studied area of chemical and pharmaceutical sciences has been the development of new biotechnological methods for obtaining enantiomers of chiral drugs with the use of enzymes as catalysts. The application of biocatalysis, which is an alternative to chemical synthesis for achieving enantiomers of chiral compounds, has received large interest from research groups and the industry. Biocatalysis does not require drastic reaction conditions, making it safer for the environment, which is consistent with the philosophy of "green chemistry". Due to the possibility of omissions of many steps of enantioselective synthesis, biocatalytic reactions give an opportunity to simplify the procedures for receiving chiral drugs.

This Special Issue, “Developments and Advances in Biocatalysis of Chiral Drugs” aims to publish high-quality manuscripts, with a special emphasis on the development of new biocatalysis approaches for creating chiral drugs, as well as the design of new chiral drugs and their applications. Since IJMS is a journal of molecular science, pure clinical or model studies will not be suitable for this Special Issue. However, clinical or pure model submissions combined with biomolecular experiments are welcome.

Dr. Tomasz Siodmiak
Guest Editor

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Keywords

  • biocatalysis
  • biotechnology
  • chiral drugs
  • chiral separation
  • enzyme
  • enzyme engineering
  • green chemistry
  • immobilization
  • support material
  • kinetic resolution

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Published Papers (1 paper)

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Research

18 pages, 860 KiB  
Article
A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives
by Joanna Siódmiak, Jacek Dulęba, Natalia Kocot, Rafał Mastalerz, Gudmundur G. Haraldsson, Michał Piotr Marszałł and Tomasz Siódmiak
Int. J. Mol. Sci. 2024, 25(10), 5084; https://doi.org/10.3390/ijms25105084 - 7 May 2024
Viewed by 1143
Abstract
The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers of chiral drugs in reactions carried out in organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it is extremely important to develop optimal procedures [...] Read more.
The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers of chiral drugs in reactions carried out in organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it is extremely important to develop optimal procedures to achieve a high enantioselectivity of the biocatalysts in the organic medium. Our paper describes a new approach to biocatalysis performed in an organic solvent with the use of CALB-octyl-agarose support including the application of a polypropylene reactor, an appropriate buffer for immobilization (Tris base—pH 9, 100 mM), a drying step, and then the storage of immobilized lipases in a climatic chamber or a refrigerator. An immobilized lipase B from Candida antarctica (CALB) was used in the kinetic resolution of (R,S)-flurbiprofen by enantioselective esterification with methanol, reaching a high enantiomeric excess (eep = 89.6 ± 2.0%). As part of the immobilization optimization, the influence of different buffers was investigated. The effect of the reactor material and the reaction medium on the lipase activity was also studied. Moreover, the stability of the immobilized lipases: lipase from Candida rugosa (CRL) and CALB during storage in various temperature and humidity conditions (climatic chamber and refrigerator) was tested. The application of the immobilized CALB in a polypropylene reactor allowed for receiving over 9-fold higher conversion values compared to the results achieved when conducting the reaction in a glass reactor, as well as approximately 30-fold higher conversion values in comparison with free lipase. The good stability of the CALB-octyl-agarose support was demonstrated. After 7 days of storage in a climatic chamber or refrigerator (with protection from humidity) approximately 60% higher conversion values were obtained compared to the results observed for the immobilized form that had not been stored. The new approach involving the application of the CALB-octyl-agarose support for reactions performed in organic solvents indicates a significant role of the polymer reactor material being used in achieving high catalytic activity. Full article
(This article belongs to the Special Issue Developments and Advances in Biocatalysis of Chiral Drugs)
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